DMSB_ECOLI
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 03-AUG-2022, entry version 169.
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 / CR34 / 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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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 dimethyl
RT 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 during
CC anaerobic growth on various sulfoxide and N-oxide 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 P18776; P18775: dmsA; NbExp=2; IntAct=EBI-1120825, EBI-4411104;
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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_STEB01000006.1.
DR AlphaFoldDB; P18776; -.
DR SMR; P18776; -.
DR BioGRID; 4260726; 3.
DR BioGRID; 849881; 2.
DR ComplexPortal; CPX-320; DmaABC 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; 67414655; -.
DR GeneID; 945507; -.
DR KEGG; ecj:JW0878; -.
DR KEGG; eco:b0895; -.
DR PATRIC; fig|1411691.4.peg.1382; -.
DR EchoBASE; EB0229; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_2_0_6; -.
DR InParanoid; P18776; -.
DR OMA; DMQRCIG; -.
DR PhylomeDB; P18776; -.
DR BioCyc; EcoCyc:DMSB-MON; -.
DR BioCyc; MetaCyc:DMSB-MON; -.
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:0005886; C:plasma membrane; IDA:ComplexPortal.
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:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0018907; P:dimethyl sulfoxide metabolic process; IDA:ComplexPortal.
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; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3062312"
FT CHAIN 2..205
FT /note="Anaerobic dimethyl sulfoxide reductase chain B"
FT /id="PRO_0000159242"
FT DOMAIN 5..33
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 59..89
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 90..119
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MUTAGEN 102
FT /note="C->F,S,W,Y: Loss of electron transfer from
FT menaquinol to DMSO."
FT /evidence="ECO:0000269|PubMed:1653010"
FT CONFLICT 170
FT /note="P -> PRA (in Ref. 1; AAA83844)"
FT /evidence="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
