GenomeNet

Database: UniProt
Entry: A7ZM48_ECO24
LinkDB: A7ZM48_ECO24
Original site: A7ZM48_ECO24 
ID   A7ZM48_ECO24            Unreviewed;       205 AA.
AC   A7ZM48;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Dimethylsulfoxide reductase, B subunit {ECO:0000313|EMBL:ABV19494.1};
GN   Name=dmsB2 {ECO:0000313|EMBL:ABV19494.1};
GN   OrderedLocusNames=EcE24377A_1796 {ECO:0000313|EMBL:ABV19494.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV19494.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV19494.1; -; Genomic_DNA.
DR   RefSeq; WP_000213015.1; NC_009801.1.
DR   AlphaFoldDB; A7ZM48; -.
DR   KEGG; ecw:EcE24377A_1796; -.
DR   HOGENOM; CLU_043374_2_0_6; -.
DR   Proteomes; UP000001122; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT   DOMAIN          5..35
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;  22768 MW;  EAE48C21000A5B2B CRC64;
     MTTQYGFFID SSRCTGCKTC ELACKDFKDL GLEVSFRRIY EYAGGDWQED NGVWHQNVFA
     YYLSISCNHC DDPACTKVCP SGAMHKREDG FVVVDEDVCI GCRYCHMACP YGAPQYNAEK
     GHMTKCDGCY SRVAEGKQPI CVESCPLRAL EFGPIEELRQ KHGTLAAVAP LPRAHFTKPN
     IVIKPNANSR PTGDTTGYLA NPEEV
//
DBGET integrated database retrieval system