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YNFH_ECOLI
ID   YNFH_ECOLI              Reviewed;         284 AA.
AC   P76173; P77142;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Anaerobic dimethyl sulfoxide reductase chain YnfH;
DE   AltName: Full=DMSO reductase anchor subunit YnfH;
GN   Name=ynfH; OrderedLocusNames=b1590, JW5261;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
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   [3]
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   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=25316676; DOI=10.1093/bioinformatics/btu671;
RA   Vlasblom J., Zuberi K., Rodriguez H., Arnold R., Gagarinova A., Deineko V.,
RA   Kumar A., Leung E., Rizzolo K., Samanfar B., Chang L., Phanse S.,
RA   Golshani A., Greenblatt J.F., Houry W.A., Emili A., Morris Q., Bader G.,
RA   Babu M.;
RT   "Novel function discovery with GeneMANIA: a new integrated resource for
RT   gene function prediction in Escherichia coli.";
RL   Bioinformatics 31:306-310(2015).
CC   -!- FUNCTION: Terminal reductase during anaerobic growth on various
CC       sulfoxide and N-oxide compounds. The C subunit anchors the other two
CC       subunits to the membrane and stabilize the catalytic subunits (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex consists of three subunits: YnfF, the reductase;
CC       YnfG, an electron transfer protein, and YnfH, a membrane anchor
CC       protein. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells grow to slightly higher density than wild-
CC       type in sublethal levels of streptomycin (PubMed:25316676).
CC       {ECO:0000269|PubMed:25316676}.
CC   -!- SIMILARITY: Belongs to the DmsC family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74662.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15314.2; -; Genomic_DNA.
DR   PIR; H64914; H64914.
DR   RefSeq; NP_416107.1; NC_000913.3.
DR   RefSeq; WP_000526503.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P76173; -.
DR   SMR; P76173; -.
DR   BioGRID; 4263479; 7.
DR   ComplexPortal; CPX-6019; Putative dimethyl sulfoxide reductase.
DR   STRING; 511145.b1590; -.
DR   TCDB; 5.A.3.3.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P76173; -.
DR   PaxDb; P76173; -.
DR   PRIDE; P76173; -.
DR   EnsemblBacteria; AAC74662; AAC74662; b1590.
DR   EnsemblBacteria; BAA15314; BAA15314; BAA15314.
DR   GeneID; 945822; -.
DR   KEGG; ecj:JW5261; -.
DR   KEGG; eco:b1590; -.
DR   PATRIC; fig|1411691.4.peg.672; -.
DR   EchoBASE; EB3607; -.
DR   eggNOG; COG3302; Bacteria.
DR   HOGENOM; CLU_064909_2_0_6; -.
DR   OMA; MMSNEIA; -.
DR   PhylomeDB; P76173; -.
DR   BioCyc; EcoCyc:G6848-MON; -.
DR   BioCyc; MetaCyc:G6848-MON; -.
DR   PRO; PR:P76173; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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:1990204; C:oxidoreductase complex; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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..284
FT                   /note="Anaerobic dimethyl sulfoxide reductase chain YnfH"
FT                   /id="PRO_0000168967"
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..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..148
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..222
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..284
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  30524 MW;  73F7D760FC4B1344 CRC64;
     MGNGWHEWPL VIFTVLGQCV VGALIVSGIG WFAAKNDADR QRIVRGMFFL WLLMGVGFIA
     SVMHLGSPLR AFNSLNRIGA SGLSNEIAAG SIFFAVGGLW WLVAVIGKMP QALGKLWLLF
     SMALGVIFVW MMTCVYQIDT VPTWHNGYTT LAFFLTVLLS GPILAAAILR AARVTFNTTP
     FAIISVLALI ACAGVIVLQG LSLASIHSSV QQASALVPDY ASLQVWRVVL LCAGLGCWLC
     PLIRRREPHV AGLILGLILI LGGEMIGRVL FYGLHMTVGM AIAG
 
 
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