GenomeNet

Database: UniProt
Entry: C0PXT2_SALPC
LinkDB: C0PXT2_SALPC
Original site: C0PXT2_SALPC 
ID   C0PXT2_SALPC            Unreviewed;       205 AA.
AC   C0PXT2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase subunit B {ECO:0000313|EMBL:ACN45132.1};
GN   Name=dmsB {ECO:0000313|EMBL:ACN45132.1};
GN   OrderedLocusNames=SPC_0965 {ECO:0000313|EMBL:ACN45132.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN45132.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN45132.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN45132.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- FUNCTION: Electron transfer subunit of the terminal reductase during
CC       anaerobic growth on various sulfoxide and N-oxide compounds.
CC       {ECO:0000256|ARBA:ARBA00003584}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000857; ACN45132.1; -; Genomic_DNA.
DR   RefSeq; WP_000213069.1; NC_012125.1.
DR   AlphaFoldDB; C0PXT2; -.
DR   KEGG; sei:SPC_0965; -.
DR   HOGENOM; CLU_043374_2_0_6; -.
DR   Proteomes; UP000001599; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16371; DMSOR_beta_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014297; DMSO_DmsB.
DR   NCBIfam; TIGR02951; DMSO_dmsB; 1.
DR   PANTHER; PTHR43177:SF5; ANAEROBIC DIMETHYL SULFOXIDE REDUCTASE CHAIN B-RELATED; 1.
DR   PANTHER; PTHR43177; PROTEIN NRFC; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12797; Fer4_2; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          5..33
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          59..89
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          90..119
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          183..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22780 MW;  B94ABE06C53C469F CRC64;
     MTTQYGFFID SSRCTGCKTC ELACKDYKDL TPDVSFRRIY EYAGGDWQED NGVWHQNVFA
     YYLSISCNHC EDPACTKVCP SGAMHKRDDG FVVVNEEVCI GCRYCHMACP YGAPQYNAAK
     GHMTKCDGCY DRVAEGKKPI CVESCPLRAL DFGPIDELRK KHGELAAVAP LPRAHFTKPN
     IVIKPNANSR PTGDTTGYLA NPKEV
//
DBGET integrated database retrieval system