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Database: UniProt
Entry: P18776
LinkDB: P18776
Original site: P18776 
ID   DMSB_ECOLI              Reviewed;         205 AA.
AC   P18776; P77745;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   10-APR-2019, entry version 153.
DE   RecName: Full=Anaerobic dimethyl sulfoxide reductase chain B;
DE   AltName: Full=DMSO reductase iron-sulfur subunit;
GN   Name=dmsB; OrderedLocusNames=b0895, JW0878;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RC   STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX   PubMed=3062312; DOI=10.1111/j.1365-2958.1988.tb00090.x;
RA   Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H.;
RT   "Nucleotide sequence of the dmsABC operon encoding the anaerobic
RT   dimethylsulphoxide reductase of Escherichia coli.";
RL   Mol. Microbiol. 2:785-795(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX   PubMed=2174699; DOI=10.1021/bi00488a030;
RA   Cammack R., Weiner J.H.;
RT   "Electron paramagnetic resonance spectroscopic characterization of
RT   dimethyl sulfoxide reductase of Escherichia coli.";
RL   Biochemistry 29:8410-8416(1990).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=1653010; DOI=10.1021/bi00098a003;
RA   Rothery R.A., Weiner J.H.;
RT   "Alteration of the iron-sulfur cluster composition of Escherichia coli
RT   dimethyl sulfoxide reductase by site-directed mutagenesis.";
RL   Biochemistry 30:8296-8305(1991).
CC   -!- FUNCTION: Electron transfer subunit of the terminal reductase
CC       during anaerobic growth on various sulfoxide and N-oxide
CC       compounds.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 4 [4Fe-4S] clusters.;
CC   -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC       (DmsAB) and a membrane anchor protein (DmsC).
CC   -!- INTERACTION:
CC       P18775:dmsA; NbExp=2; IntAct=EBI-1120825, EBI-4411104;
DR   EMBL; J03412; AAA83844.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73981.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35627.1; -; Genomic_DNA.
DR   PIR; F64828; F64828.
DR   RefSeq; NP_415415.1; NC_000913.3.
DR   RefSeq; WP_000213098.1; NZ_LN832404.1.
DR   ProteinModelPortal; P18776; -.
DR   SMR; P18776; -.
DR   BioGrid; 4260726; 3.
DR   ComplexPortal; CPX-320; DMSO reductase complex.
DR   DIP; DIP-9453N; -.
DR   IntAct; P18776; 6.
DR   STRING; 511145.b0895; -.
DR   TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P18776; -.
DR   PaxDb; P18776; -.
DR   PRIDE; P18776; -.
DR   EnsemblBacteria; AAC73981; AAC73981; b0895.
DR   EnsemblBacteria; BAA35627; BAA35627; BAA35627.
DR   GeneID; 945507; -.
DR   KEGG; ecj:JW0878; -.
DR   KEGG; eco:b0895; -.
DR   PATRIC; fig|1411691.4.peg.1382; -.
DR   EchoBASE; EB0229; -.
DR   EcoGene; EG10233; dmsB.
DR   eggNOG; ENOG4105QAX; Bacteria.
DR   eggNOG; COG0437; LUCA.
DR   HOGENOM; HOG000163387; -.
DR   InParanoid; P18776; -.
DR   KO; K07307; -.
DR   PhylomeDB; P18776; -.
DR   BioCyc; EcoCyc:DMSB-MONOMER; -.
DR   BioCyc; ECOL316407:JW0878-MONOMER; -.
DR   BioCyc; MetaCyc:DMSB-MONOMER; -.
DR   PRO; PR:P18776; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
DR   GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014297; DMSO_DmsB.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12800; Fer4_4; 1.
DR   TIGRFAMs; TIGR02951; DMSO_dmsB; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3062312}.
FT   CHAIN         2    205       Anaerobic dimethyl sulfoxide reductase
FT                                chain B.
FT                                /FTId=PRO_0000159242.
FT   DOMAIN        5     33       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       59     89       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       90    119       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        20     20       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        24     24       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        67     67       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        70     70       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        75     75       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        79     79       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        99     99       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       102    102       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       105    105       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       109    109       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       126    126       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       129    129       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       141    141       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       145    145       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   MUTAGEN     102    102       C->F,S,W,Y: Loss of electron transfer
FT                                from menaquinol to DMSO.
FT                                {ECO:0000269|PubMed:1653010}.
FT   CONFLICT    170    170       P -> PRA (in Ref. 1; AAA83844).
FT                                {ECO:0000305}.
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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