DMSC_ECOLI
ID DMSC_ECOLI Reviewed; 287 AA.
AC P18777;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Anaerobic dimethyl sulfoxide reductase chain C;
DE AltName: Full=DMSO reductase anchor subunit;
GN Name=dmsC; OrderedLocusNames=b0896, JW0879;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 TOPOLOGY.
RX PubMed=8429002; DOI=10.1016/s0021-9258(18)53684-x;
RA Weiner J.H., Shaw G., Turner R.J., Trieber C.A.;
RT "The topology of the anchor subunit of dimethyl sulfoxide reductase of
RT Escherichia coli.";
RL J. Biol. Chem. 268:3238-3244(1993).
RN [6]
RP TOPOLOGY.
RX PubMed=2170332; DOI=10.1128/jb.172.10.5938-5948.1990;
RA Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H.;
RT "Organization of dimethyl sulfoxide reductase in the plasma membrane of
RT Escherichia coli.";
RL J. Bacteriol. 172:5938-5948(1990).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Terminal reductase during anaerobic growth on various
CC sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the
CC membrane and stabilizes it.
CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC (DmsAB) and a membrane anchor protein (DmsC).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the DmsC family. {ECO:0000305}.
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DR EMBL; J03412; AAA83845.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73982.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35628.1; -; Genomic_DNA.
DR PIR; S03787; S03787.
DR RefSeq; NP_415416.1; NC_000913.3.
DR RefSeq; WP_000534637.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P18777; -.
DR SMR; P18777; -.
DR BioGRID; 4260727; 5.
DR ComplexPortal; CPX-320; DmaABC DMSO reductase complex.
DR IntAct; P18777; 1.
DR STRING; 511145.b0896; -.
DR TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P18777; -.
DR PaxDb; P18777; -.
DR PRIDE; P18777; -.
DR EnsemblBacteria; AAC73982; AAC73982; b0896.
DR EnsemblBacteria; BAA35628; BAA35628; BAA35628.
DR GeneID; 66670830; -.
DR GeneID; 945502; -.
DR KEGG; ecj:JW0879; -.
DR KEGG; eco:b0896; -.
DR PATRIC; fig|1411691.4.peg.1381; -.
DR EchoBASE; EB0230; -.
DR eggNOG; COG3302; Bacteria.
DR HOGENOM; CLU_064909_2_0_6; -.
DR OMA; MVRVYNT; -.
DR PhylomeDB; P18777; -.
DR BioCyc; EcoCyc:DMSC-MON; -.
DR BioCyc; MetaCyc:DMSC-MON; -.
DR PRO; PR:P18777; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IDA:EcoCyc.
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; IPR007059; DmsC.
DR PANTHER; PTHR38095; PTHR38095; 1.
DR Pfam; PF04976; DmsC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..287
FT /note="Anaerobic dimethyl sulfoxide reductase chain C"
FT /id="PRO_0000079947"
FT TOPO_DOM 1..9
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 33..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 67..89
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 108..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 135..156
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 175..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 202..224
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..242
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 243..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..280
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 281..287
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 30826 MW; DB6D26ACD2BE0CEB CRC64;
MGSGWHEWPL MIFTVFGQCV AGGFIVLALA LLKGDLRAEA QQRVIACMFG LWVLMGIGFI
ASMLHLGSPM RAFNSLNRVG ASALSNEIAS GSIFFAVGGI GWLLAMLKKL SPALRTLWLI
VTMVLGVIFV WMMVRVYNSI DTVPTWYSIW TPMGFFLTMF MGGPLLGYLL LSLAGVDGWA
MRLLPAISVL ALVVSGVVSV MQGAELATIH SSVQQAAALV PDYGALMSWR IVLLAVALCL
WIAPQLKGYQ PAVPLLSVSF ILLLAGELIG RGVFYGLHMT VGMAVAS
