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Database: UniProt
Entry: Q3Z3M5_SHISS
LinkDB: Q3Z3M5_SHISS
Original site: Q3Z3M5_SHISS 
ID   Q3Z3M5_SHISS            Unreviewed;       205 AA.
AC   Q3Z3M5;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase subunit B {ECO:0000313|EMBL:AAZ87637.1};
GN   Name=dmsB {ECO:0000313|EMBL:AAZ87637.1};
GN   OrderedLocusNames=SSON_0896 {ECO:0000313|EMBL:AAZ87637.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87637.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87637.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87637.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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};
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DR   EMBL; CP000038; AAZ87637.1; -; Genomic_DNA.
DR   RefSeq; WP_000213098.1; NC_007384.1.
DR   AlphaFoldDB; Q3Z3M5; -.
DR   SMR; Q3Z3M5; -.
DR   GeneID; 83577170; -.
DR   KEGG; ssn:SSON_0896; -.
DR   HOGENOM; CLU_043374_2_0_6; -.
DR   Proteomes; UP000002529; 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:UP000002529}.
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          184..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22869 MW;  7EC4417EED0809C6 CRC64;
     MTTQYGFFID SSRCTGCKTC ELACKDYKDL TPEVSFRRIY EYAGGDWQED NGVWHQNVFA
     YYLSISCNHC EDPACTKVCP SGAMHKREDG FVVVDEDVCI GCRYCHMACP YGAPQYNETK
     GHMTKCDGCY DRVAEGKKPI CVESCPLRAL DFGPIDELRK KHGDLAAVAP LPRAHFTKPN
     IVIKPNANSR PTGDTTGYLA NPKEV
//
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