1VZ0,1VZ0,1VZ0,4UMK


Conserved Protein Domain Family
SPO0J_N

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cd16393: SPO0J_N 
Click on image for an interactive view with Cn3D
Thermus thermophilus stage 0 sporulation protein J-like N-terminal domain, ParB family member
Spo0J (stage 0 sporulation protein J) is a ParB family member, a critical component of the ParABS-type bacterial chromosome segregation system. The Spo0J N-terminal region acts in protein-protein interaction and is adjacent to the DNA-binding domain that binds to parS sites. Two Spo0J bind per parS site, and Spo0J interacts with neighbors via the N-terminal domain to form oligomers via an Arginine-rich patch (RRXR). This superfamily represents the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system. parABS contributes to the efficient segregation of chromosomes and low-copy number plasmids to daughter cells during prokaryotic cell division. The process includes the parA (Walker box) ATPase, the ParB DNA-binding protein and a parS cis-acting DNA sites. Binding of ParB to centromere-like parS sites is followed by non-specific binding to DNA ("spreading", which has been implicated in gene silencing in plasmid P1) and oligomerization of additional ParB molecules near the parS sites. It has been proposed that ParB-ParB cross-linking compacts the DNA, binds to parA via the N-terminal region, and leads to parA separating the ParB-parS complexes and the recruitment of the SMC (structural maintenance of chromosomes) complexes. The ParB N-terminal domain of Bacillus subtilis and other species contains a Arginine-rich ParB Box II with residues essential for bridging of the ParB-parS complexes. The arginine-rich ParB Box II consensus (I[VIL]AGERR[FYW]RA[AS] identified in several species is partially conserved with this family and related families. Mutations within the basic columns particularly debilitate spreading from the parS sites and impair SMC recruitment. The C-terminal domain contains a HTH DNA-binding motif and is the primary homo-dimerization domain, and binds to parS DNA sites. Additional homo-dimerization contacts are found along the N-terminal domain, but dimerization of the N-terminus may only occur after concentration at ParB-parS foci.
Statistics
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PSSM-Id: 319251
Aligned: 65 rows
Threshold Bit Score: 123.748
Created: 21-May-2015
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
arginine patchputative ParB
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1: arginine patch [polypeptide binding site], 3 residue positions
Conserved feature residue pattern:R R RClick to see conserved feature residue pattern help
Evidence:
  • Comment:arginine patch mediates adjacent and transverse oligomerization
  • Comment:third residue typically hydrophobic
  • Comment:arginine patch shown to be critical for "spreading" in vivo and DNA-bridging in vitro in Bacillus subtilis

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                              ## #      
1VZ0_G        23 VVRLPLASIRPNPrQPRKRFAEESLKELADSIREKGLLQPLLVRPqg--------------dGYELVAGERRYRAALMAG 88  Thermus thermop...
YP_003971885 172 LLDIPVSSIVPNAqQPRSVFDEEELNELAASIKEVGVLQPIVVRKrqagessksdvsretsqRYELIMGERRWRASQLAQ 251 Bifidobacterium...
Q50201        60 YREIALSDITENPcQPRQVFDDEAMSELVHSIREFGLLQPIVVRPasgs---------cgdtRYQIVMGERRWRAAQQAG 130 Mycobacterium l...
EFL82261      29 MRDVGVEVIKADPrQPRKEFDEEALKELAESIKAHGLIQPIVLRPspd-----------kedEYYIIAGERRFRAVKLNG 97  Burkholderiales...
EFE27953       3 LQTIELQKIIPDPcQPRKFFDLAALEELASSIEQYGLLSPIIVRKqg--------------dRYIIVAGERRYRAMLLNK 68  Filifactor aloc...
NP_628073     45 FAEVPLDAITPNPkQPRKDFDDDALAELVTSIREVGLLQPVVVRPte-------------pgRYELIMGERRFRACRELE 111 Streptomyces co...
EFW01948      26 VLEIALDKIERDEsQPRKNFDEDTLRDLAESIEAYGLLQPIVIRKkpn-----------aldRYIIVAGERRYRASQLLK 94  Sutterella wads...
EMG12052      51 VQNIPVSKIISKE-NPRKNFNSESLQELAESIKKYGLIQPISVRKig--------------nEYHLIAGERRLRATKLNG 115 Leptospira inte...
EEI86305      37 VASLPIEKVKPRPgQPRKDFDSKALEDLAHSIKEYGLLNPITVTKng--------------dYYEILAGERRYRATLLNQ 102 Anaerococcus la...
EKA71931       8 YQDLDINLIKPDPeQPRKIFEDDSLTDLSNSIKATGVKQPITVRKvn--------------nEYMIIAGERRYRASILAN 73  Acinetobacter b...
Feature 1                                           
1VZ0_G        89 LQEVPAVVKDL----TDREa-lELALVENLQREDL 118 Thermus thermophilus HB27
YP_003971885 252 LKTIPAIVKTTs---DDEMl--RDALLENLHRVAL 281 Bifidobacterium bifidum
Q50201       131 LSFIPAIVRATg---DDSMl--RDALLENIHRVQL 160 Mycobacterium leprae
EFL82261      98 DKTIRAIVKKTl---KPEEi-gYVQMAENIKRANL 128 Burkholderiales bacterium 1_1_47
EFE27953      69 MTHANCIVRNH----IDFR---EVSLIENVQREDL 96  Filifactor alocis ATCC 35896
NP_628073    112 LDAIPAIVRATe---DEKLl--LDALLENLHRAQL 141 Streptomyces coelicolor
EFW01948      95 ARTIKAVLLETn--pDDAEl-gYLQVIENIKRDAL 126 Sutterella wadsworthensis 3_1_45B
EMG12052     116 EEFISSIVKNVh--qVDPDlipEYKLIENIHREDL 148 Leptospira interrogans serovar Grippotyphosa str. LT2186
EEI86305     103 ADTIDAIVKTYe--qKDIE---VLSLIENVQREDL 132 Anaerococcus lactolyticus ATCC 51172
EKA71931      74 KTTIPAVIIGDesqlTEEAl-yAHQLNENLHREDL 107 Acinetobacter baumannii IS-58

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