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Conserved domains on  [gi|2564982702|ref|WP_306174120|]
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MULTISPECIES: murein hydrolase activator NlpD [Enterobacteriaceae]

Protein Classification

murein hydrolase activator NlpD( domain architecture ID 11485035)

murein hydrolase activator NlpD is required for septal murein cleavage and daughter cell separation during cell division

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
2-364 0e+00

murein hydrolase activator NlpD;


:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 520.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702   2 SLVSLWLAGCSDTSNPPAPVSSVNgnapantnsgmlitpppkmgttstaqqpqiqpvqqpqiqatqqpqiqpvqpvaqqp 81
Cdd:PRK10871   17 SLVSLWLAGCSNTSNPPAPVSSVG-------------------------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702  82 vqmeNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITGG 161
Cdd:PRK10871   41 ----NGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASGTPITGG 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 162 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTSTSTP 241
Cdd:PRK10871  117 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTEPTASSTSTSTP 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 242 ISTWRWPTEGKVIETFGASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 321
Cdd:PRK10871  197 ISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2564982702 322 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 364
Cdd:PRK10871  277 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
2-364 0e+00

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 520.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702   2 SLVSLWLAGCSDTSNPPAPVSSVNgnapantnsgmlitpppkmgttstaqqpqiqpvqqpqiqatqqpqiqpvqpvaqqp 81
Cdd:PRK10871   17 SLVSLWLAGCSNTSNPPAPVSSVG-------------------------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702  82 vqmeNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITGG 161
Cdd:PRK10871   41 ----NGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASGTPITGG 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 162 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTSTSTP 241
Cdd:PRK10871  117 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTEPTASSTSTSTP 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 242 ISTWRWPTEGKVIETFGASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 321
Cdd:PRK10871  197 ISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2564982702 322 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 364
Cdd:PRK10871  277 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 245-364 2.13e-51

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 175.34  E-value: 2.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 245 WRWPTEGKVIETFGASEGG---NKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 321
Cdd:COG4942   255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2564982702 322 QQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLRYLPQR 364
Cdd:COG4942   334 GQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 262-357 7.31e-41

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 138.83  E-value: 7.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 262 GGNKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 341
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 2564982702 342 -TRLHFEIRYKGKSVNP 357
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 264-348 7.60e-30

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 109.60  E-value: 7.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 264 NKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-T 342
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                  ....*.
gi 2564982702 343 RLHFEI 348
Cdd:cd12797    80 HLHFEI 85
LysM smart00257
Lysin motif;
107-150 8.47e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.30  E-value: 8.47e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2564982702  107 TYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQV 150
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
2-364 0e+00

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 520.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702   2 SLVSLWLAGCSDTSNPPAPVSSVNgnapantnsgmlitpppkmgttstaqqpqiqpvqqpqiqatqqpqiqpvqpvaqqp 81
Cdd:PRK10871   17 SLVSLWLAGCSNTSNPPAPVSSVG-------------------------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702  82 vqmeNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITGG 161
Cdd:PRK10871   41 ----NGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASGTPITGG 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 162 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTSTSTP 241
Cdd:PRK10871  117 NAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTEPTASSTSTSTP 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 242 ISTWRWPTEGKVIETFGASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 321
Cdd:PRK10871  197 ISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2564982702 322 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 364
Cdd:PRK10871  277 QQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 245-364 2.13e-51

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 175.34  E-value: 2.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 245 WRWPTEGKVIETFGASEGG---NKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 321
Cdd:COG4942   255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2564982702 322 QQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLRYLPQR 364
Cdd:COG4942   334 GQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 246-363 7.00e-48

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 160.52  E-value: 7.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 246 RWPTEGKVIETFGA-------SEGGNKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTML 318
Cdd:COG0739    72 AWPVKGRITSGFGYrrhpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTLYAHLSSIL 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2564982702 319 VREQQEVKAGQKIATMGSTGTSS-TRLHFEIRYKGKSVNPLRYLPQ 363
Cdd:COG0739   151 VKVGQRVKAGQVIGYVGNTGRSTgPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 262-357 7.31e-41

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 138.83  E-value: 7.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 262 GGNKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 341
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 2564982702 342 -TRLHFEIRYKGKSVNP 357
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 264-348 7.60e-30

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 109.60  E-value: 7.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 264 NKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-T 342
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                  ....*.
gi 2564982702 343 RLHFEI 348
Cdd:cd12797    80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 247-363 1.35e-27

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 107.42  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 247 WPTEGKVIETFGA----SEGGN-----KGIDIAGSKGQAIIATADGRVVYAGNALRgYGNLIIIKHNDDYLSAYAH-NDT 316
Cdd:COG5821    71 KPVSGKITREFGEdlvySKTLNewrthTGIDIAAKEGTPVKAAADGVVVEVGKDPK-YGITVVIDHGNGIKTVYANlDSK 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2564982702 317 MLVREQQEVKAGQKIATMGSTG--TSST--RLHFEIRYKGKSVNPLRYLPQ 363
Cdd:COG5821   150 IKVKVGQKVKKGQVIGKVGSTAlfESSEgpHLHFEVLKNGKPVDPMKYLKK 200
PRK11637 PRK11637
AmiB activator; Provisional
 247-361 3.57e-23

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 99.77  E-value: 3.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 247 WPTEGKVIETFGASEGGN---KGIDIAGSKGQAIIATADGRVVYAgNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQ 323
Cdd:PRK11637  309 WPVRGPTLHRFGEQLQGElrwKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGA 387

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2564982702 324 EVKAGQKIATMGSTGTSST-RLHFEIRYKGKSVNPLRYL 361
Cdd:PRK11637  388 QVRAGQPIALVGSSGGQGRpSLYFEIRRQGQAVNPQPWL 426
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 248-362 1.40e-19

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 86.20  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 248 PTEGKVIETFGasEGGnKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKA 327
Cdd:COG5833   107 PVSGKVVESFQ--ENG-KGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEA 182

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2564982702 328 GQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLP 362
Cdd:COG5833   183 GQKIGTVPATEGEEGTFYFAIKKGGKFIDPIQVIS 217
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 264-363 1.74e-15

Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444522 [Multi-domain]  Cd Length: 224  Bit Score: 74.57  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 264 NKGIDIAGSKGQA--IIATADGRVVYAGN-ALrgYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGST--- 337
Cdd:COG5820   120 STGIDIAAKDGESfdVLAALSGTVTEVEEdPL--LGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNlfn 197

                          90       100
                  ....*....|....*....|....*.
gi 2564982702 338 GTSSTRLHFEIRYKGKSVNPLRYLPQ 363
Cdd:COG5820   198 KDAGVHLHFEVRKDGKAVNPESYLPK 223
PRK11649 PRK11649
putative peptidase; Provisional
 265-358 5.12e-14

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 72.78  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 265 KGIDIAGSKGQAIIATADGRVV---YAGNAlrgyGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 341
Cdd:PRK11649  314 RGVDFAMPVGTPVLAVGDGEVVvakRSGAA----GNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRST 389

                          90
                  ....*....|....*...
gi 2564982702 342 -TRLHFEIRYKGKSVNPL 358
Cdd:PRK11649  390 gPHLHYEVWINQQAVNPL 407
LysM smart00257
Lysin motif;
107-150 8.47e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.30  E-value: 8.47e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2564982702  107 TYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQV 150
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 108-150 2.35e-09

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 52.40  E-value: 2.35e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2564982702 108 YTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYaLNVGQTLQV 150
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 107-150 3.41e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 52.10  E-value: 3.41e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2564982702 107 TYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQV 150
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 104-190 6.56e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 50.89  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 104 SGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPyALNVGQTLQVGNASGTP--ITGGNAIT----QAD-----AAEQ 172
Cdd:PRK10783  342 NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-KLKVGQTLTIGAGSSAQrlANNSDSITyrvrKGDslssiAKRH 420

                          90       100
                  ....*....|....*....|
gi 2564982702 173 GVVIKPAQ--NSTVAVASQP 190
Cdd:PRK10783  421 GVNIKDVMrwNSDTAKNLQP 440
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
93-150 1.67e-05

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 44.70  E-value: 1.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564982702  93 RQYGNIPKGSYSgsTYTVKKGDTLFYIAWITGNDFRDLAQRNNIqAPYALNVGQTLQV 150
Cdd:COG1388    99 RRYGAAAAPSPV--TYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKI 153
PRK00566 PRK00566
DNA-directed RNA polymerase subunit beta'; Provisional
 266-331 2.03e-03

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 234794 [Multi-domain]  Cd Length: 1156  Bit Score: 40.05  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702  266 GIDIAGS-------------KGQAIIATADGRVVYaGNALRGYGNLIIIKHNDD---YL-SAYAHndtMLVREQQEVKAG 328
Cdd:PRK00566   906 GVDITGGlprvaelfearkpKGPAIIAEIDGTVSF-GKETKGKRRIVITPDDGEereYLiPKGKH---LLVQEGDHVEAG 981


                   ...
gi 2564982702  329 QKI 331
Cdd:PRK00566   982 DKL 984
PRK06148 PRK06148
hypothetical protein; Provisional
 266-348 2.36e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.01  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702  266 GIDIAGSKGQAIIATADGRVVYAGN-ALR-GYGNLIIIKHN----DDYLSAYAHNDTMLV---REQQEVKAGQKIATMGS 336
Cdd:PRK06148   443 GVDLFAPAGTPVYAPLAGTVRSVEIeAVPlGYGGLVALEHEtpggDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGD 522

                           90
                   ....*....|....*
gi 2564982702  337 TGTSSTR---LHFEI 348
Cdd:PRK06148   523 AHENGGWaphLHFQL 537
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 104-150 2.80e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 38.06  E-value: 2.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2564982702 104 SGSTYTVKKGDTLFYIAWI---TGNDFRDLAQRN--NIQAPYALNVGQTLQV 150
Cdd:COG1652   108 APKTYTVKPGDTLWGIAKRfygDPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
PRK13914 PRK13914
invasion associated endopeptidase;
104-193 6.40e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 38.24  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564982702 104 SGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPyALNVGQTLQVGNASGTPITGGNAITQADAAEQGV--VIKPAQN 181
Cdd:PRK13914  198 NATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSS-SIYVGQKLAIKQTANTATPKAEVKTEAPAAEKQAapVVKENTN 276

                          90
                  ....*....|..
gi 2564982702 182 STVAVASQPTIT 193
Cdd:PRK13914  277 TNTATTEKKETT 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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