DMSC_HAEIN
ID DMSC_HAEIN Reviewed; 279 AA.
AC P45002; Q48050;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Anaerobic dimethyl sulfoxide reductase chain C;
DE AltName: Full=DMSO reductase anchor subunit;
GN Name=dmsC; OrderedLocusNames=HI_1045;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Eagan / Serotype B;
RX PubMed=8635740; DOI=10.1016/0378-1119(95)00808-x;
RA Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.;
RT "Sequences of the genes encoding the A, B and C subunits of the Haemophilus
RT influenzae dimethylsulfoxide reductase complex.";
RL Gene 169:137-138(1996).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DmsC family. {ECO:0000305}.
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DR EMBL; L42023; AAC22704.1; -; Genomic_DNA.
DR EMBL; U26665; AAB06235.1; -; Genomic_DNA.
DR PIR; E64109; E64109.
DR RefSeq; NP_439204.1; NC_000907.1.
DR RefSeq; WP_005693381.1; NC_000907.1.
DR AlphaFoldDB; P45002; -.
DR SMR; P45002; -.
DR STRING; 71421.HI_1045; -.
DR EnsemblBacteria; AAC22704; AAC22704; HI_1045.
DR KEGG; hin:HI_1045; -.
DR PATRIC; fig|71421.8.peg.1090; -.
DR eggNOG; COG3302; Bacteria.
DR HOGENOM; CLU_064909_2_0_6; -.
DR OMA; MMSNEIA; -.
DR PhylomeDB; P45002; -.
DR BioCyc; HINF71421:G1GJ1-1084-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IBA:GO_Central.
DR GO; GO:0019645; P:anaerobic electron transport chain; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR InterPro; IPR007059; DmsC.
DR PANTHER; PTHR38095; PTHR38095; 1.
DR Pfam; PF04976; DmsC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..279
FT /note="Anaerobic dimethyl sulfoxide reductase chain C"
FT /id="PRO_0000079948"
FT TOPO_DOM 1..9
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..86
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..150
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..219
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..279
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT VARIANT 21
FT /note="V -> A (in strain: Eagan)"
FT VARIANT 276
FT /note="T -> A (in strain: Eagan)"
SQ SEQUENCE 279 AA; 30756 MW; 892D1AFBC08867BF CRC64;
MNTGLYELPL VFFTVLAQSA VGAWLVFTFV LLNEKNTKSR TYIHKVMFVI LALLGIGFIA
SIMHLGLPIR AFNSLNRVGS SMMSNEIAAG AIFFTLAGFY WLIAILGKMP VSLGNVWRIV
TALIGILFMY VMNQVYHITS IPTWNNALTS WSFYLTVVLG GLTLSYALLI PNKQREYQLQ
HLPSLFAIGV SLVAIVAIYQ GFNLHNIHSA IQNAADLVPN YAIMTVTRLC LLSIVAFLLF
RVKNIGLLGI SVLLTLVAEG IGRVLFYGLH MTYGMTIGG
