2HQV,2OVI,2PH0


Conserved Protein Domain Family
ChuX_HutX-like

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cd16829: ChuX_HutX-like 
Click on image for an interactive view with Cn3D
heme iron utilization protein ChuX and similar proteins
This family contains proteins similar to ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and includes ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade. ChuX, a member of the conserved heme utilization operon from pathogenic E. coli O157:H7, forms a dimer with a very similar fold to the monomer structure of two other heme utilization proteins, ChuS and HemS, despite low sequence homology. ChuX has been shown to bind heme in a 1:1 manner, inferring that the ChuX homodimer could coordinate two heme molecules in contrast to only one heme molecule bound in ChuS and HemS. Similarly, cytoplasmic heme-binding protein HutX in Vibrio cholera, an intracellular heme transport protein for the heme-degrading enzyme HutZ, forms a dimer, each domain binding heme that is transferred from HutX to HutZ via a specific protein-protein interaction. This family also includes AGR_C_4470p from Agrobacterium tumefaciens and found to be a dimer, with each subunit having strong structural homology and organization to the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. However, the heme binding site is not conserved in AGR_C_4470p, suggesting a possible different function.
Statistics
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PSSM-Id: 319358
View PSSM: cd16829
Aligned: 83 rows
Threshold Bit Score: 164.595
Threshold Setting Gi: 917032983
Created: 5-Jul-2016
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfaceheme binding
Conserved site includes 16 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                             #   #######                
2HQV_A        42 EAIAAKAEv--aPAEILAILpqgAAVSAPa---dRFDAIWNEXRGWGe-ILXIVQTgDIVLEVPgHLPEGTEShGWFNIH 115
2OVI_A        17 TLEVVAEQynttLLEVVRNLp--SSTVVPg---dKFDTVWDTVCEWGn-VTTLVHTaDVILEFSgELPSGFHRhGYFNLR 90
gi 316921726  27 MLASLAERfgvsELEVARALp-dEARAFAgk--dAFDTVWQALASWEn-ATFIMAHlGSVIEIKgKIPEGRHGhGYFNLS 102
gi 316947264  23 MLSQLAREhgleEGQIMPLLspdMAVAVPa---dHFMDLWKEISQWKr-ITFIVVNeGMVVEVKgTLPQGSSGhGMFNLH 98
gi 322417537  21 GLQMLAGVcrksELEVIKALpegMGMLFEg---sYFDKVWQMLTEIDt-LTFFIESsGNIFEFKtKVEHGREGfGYFNLF 96
gi 378598221  25 TFGSVAKAlgvtPCEAAQLLpesVTAFVAgdaseRFAEIWEMLASWEkvTLFIIHA-GNVFEIEgKLHTGKIAqGYYNIL 103
gi 524142549  28 TVSSIAGRlgvtDLEAAELLpeaNCTFVKgditeRFIEIWAELASWEk-ITLFIQHeGSIFEIQgQLHEGKIAqGYYNIL 106
gi 524661053  26 TLATVAKAlnttELASAQKMpddAVAFVTgsiaeRFEALWAELASWQkvTLFIVHA-GHVFEIQtKLSTGKCArGYYNIL 104
gi 524781680  18 TLGLIARElgcsDLEAARALpaeNCSFIKdi--nMFDDLWSEMSQWEkvTLFIIHE-GHVFEIQsKLSAGKRAmGYYNIL 94
gi 550905452  24 MLDTLAQAcgvsELQAAEALpqpMRVFAAa---aDFDAIWADLTAWEs-ATFIMRHgGSVVEIKgQIPAGKHGgGYFNLD 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
Feature 1             ######                         #     #                          
2HQV_A       116 Gds-pIGGHIKKdncaAITFVDRGFhgRRSCSVWFXNaaGGAXFKIFVRRDen-kELLAGQLAKFEELR 182
2OVI_A        91 Gkh-gMSGHIKAenctHIALIERKFmgMDTASILFFNkeGSAMLKIFLGRDdh-rQLLSEQVSAFHTLA 157
gi 316921726 103 Ggs-gLGGHLKIddlgHICFLSLPFmgLESHSVQFFNaaGTVLFSVYVGREn--rQLIPAARESFFALR 168
gi 316947264  99 EadnpLGGHIFIgklgSIWLLSKPHfgVESHSVHFFTreNKPMFAVYVGRDpetrQLLEEVKNHFLTLK 167
gi 322417537  97 Gkn-cLNGHLRKetvsSIALLKIPFmqLESRQVAFINtdGKVMYSFYLPREg--qKIDPKAEELFNAFI 162
gi 378598221 104 SkhatIGGHLNYqdvaAVCFAELPFmgRESLSVQFFNkaGEAAFAVYAGREn--hQIIPSVKEAFFAAK 170
gi 524142549 107 AksatIGGHMKYdsfsAVAFTTFPFmgRESLAVQFFTkeGKTAFSVFVGREn--hQLVESVKEKFIAAR 173
gi 524661053 105 QkdavAGGHIKYeviaAAAFVTMPFmgRESHSVQFFCndGSVAFSVYVGREn--hQLIDSVVEAFHKAK 171
gi 524781680  95 AkdavIGGHINPdsleTAAFISMPFmgRESHYVAFFGkdQKLHFCIYVGREn--hQLIESVKEGFLKAK 161
gi 550905452 100 Hgc-pLGGHICSnniaHMAFLSLPFmgLESHSIQFFDaaGAVVFSIYVGREn--rALIPSVKERFLALR 165

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