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Anaerobic dimethyl sulfoxide reductase chain C (DMSO reductase anchor subunit)

 DMSC_ECOLI              Reviewed;         287 AA.
P18777;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
20-JUN-2018, entry version 131.
RecName: Full=Anaerobic dimethyl sulfoxide reductase chain C;
AltName: Full=DMSO reductase anchor subunit;
Name=dmsC; OrderedLocusNames=b0896, JW0879;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=3062312; DOI=10.1111/j.1365-2958.1988.tb00090.x;
Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H.;
"Nucleotide sequence of the dmsABC operon encoding the anaerobic
dimethylsulphoxide reductase of Escherichia coli.";
Mol. Microbiol. 2:785-795(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
TOPOLOGY.
PubMed=8429002;
Weiner J.H., Shaw G., Turner R.J., Trieber C.A.;
"The topology of the anchor subunit of dimethyl sulfoxide reductase of
Escherichia coli.";
J. Biol. Chem. 268:3238-3244(1993).
[6]
TOPOLOGY.
PubMed=2170332; DOI=10.1128/jb.172.10.5938-5948.1990;
Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H.;
"Organization of dimethyl sulfoxide reductase in the plasma membrane
of Escherichia coli.";
J. Bacteriol. 172:5938-5948(1990).
[7]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
-!- FUNCTION: Terminal reductase during anaerobic growth on various
sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to
the membrane and stabilizes it.
-!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
(DmsAB) and a membrane anchor protein (DmsC).
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- SIMILARITY: To E.coli YnfH. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03412; AAA83845.1; -; Genomic_DNA.
EMBL; U00096; AAC73982.1; -; Genomic_DNA.
EMBL; AP009048; BAA35628.1; -; Genomic_DNA.
PIR; S03787; S03787.
RefSeq; NP_415416.1; NC_000913.3.
RefSeq; WP_000534637.1; NZ_LN832404.1.
ProteinModelPortal; P18777; -.
BioGrid; 4260727; 5.
ComplexPortal; CPX-320; DMSO reductase complex.
IntAct; P18777; 1.
STRING; 316385.ECDH10B_0966; -.
TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P18777; -.
PRIDE; P18777; -.
EnsemblBacteria; AAC73982; AAC73982; b0896.
EnsemblBacteria; BAA35628; BAA35628; BAA35628.
GeneID; 945502; -.
KEGG; ecj:JW0879; -.
KEGG; eco:b0896; -.
PATRIC; fig|1411691.4.peg.1381; -.
EchoBASE; EB0230; -.
EcoGene; EG10234; dmsC.
eggNOG; ENOG4107KGK; Bacteria.
eggNOG; COG3302; LUCA.
HOGENOM; HOG000118381; -.
KO; K07308; -.
OMA; MVRVYNT; -.
BioCyc; EcoCyc:DMSC-MONOMER; -.
BioCyc; MetaCyc:DMSC-MONOMER; -.
PRO; PR:P18777; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IDA:EcoCyc.
GO; GO:0019645; P:anaerobic electron transport chain; IEA:InterPro.
GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
InterPro; IPR007059; DmsC.
PANTHER; PTHR38095; PTHR38095; 1.
Pfam; PF04976; DmsC; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Membrane;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 287 Anaerobic dimethyl sulfoxide reductase
chain C.
/FTId=PRO_0000079947.
TOPO_DOM 1 9 Periplasmic. {ECO:0000305}.
TRANSMEM 10 32 Helical. {ECO:0000305}.
TOPO_DOM 33 43 Cytoplasmic. {ECO:0000305}.
TRANSMEM 44 66 Helical. {ECO:0000305}.
TOPO_DOM 67 89 Periplasmic. {ECO:0000305}.
TRANSMEM 90 107 Helical. {ECO:0000305}.
TOPO_DOM 108 114 Cytoplasmic. {ECO:0000305}.
TRANSMEM 115 134 Helical. {ECO:0000305}.
TOPO_DOM 135 156 Periplasmic. {ECO:0000305}.
TRANSMEM 157 174 Helical. {ECO:0000305}.
TOPO_DOM 175 182 Cytoplasmic. {ECO:0000305}.
TRANSMEM 183 201 Helical. {ECO:0000305}.
TOPO_DOM 202 224 Periplasmic. {ECO:0000305}.
TRANSMEM 225 242 Helical. {ECO:0000305}.
TOPO_DOM 243 254 Cytoplasmic. {ECO:0000305}.
TRANSMEM 255 280 Helical. {ECO:0000305}.
TOPO_DOM 281 287 Periplasmic. {ECO:0000305}.
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


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