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TTRC_ARCFU
ID   TTRC_ARCFU              Reviewed;         361 AA.
AC   O30079;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Tetrathionate reductase subunit C;
GN   Name=ttrC; OrderedLocusNames=AF_0158;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   GENE NAME.
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=22289056; DOI=10.1021/bi201852d;
RA   Coulthurst S.J., Dawson A., Hunter W.N., Sargent F.;
RT   "Conserved signal peptide recognition systems across the prokaryotic
RT   domains.";
RL   Biochemistry 51:1678-1686(2012).
CC   -!- FUNCTION: Part of a membrane-bound tetrathionate reductase that
CC       catalyzes the reduction of tetrathionate to thiosulfate. TtrC probably
CC       anchors TtrA and TtrB to the external face of the cytoplasmic membrane.
CC       May transfer electrons from membrane quinol to TtrB (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Probably composed of three subunits: TtrA, TtrB and TtrC.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NrfD family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB91076.1; -; Genomic_DNA.
DR   PIR; F69269; F69269.
DR   RefSeq; WP_010877670.1; NC_000917.1.
DR   AlphaFoldDB; O30079; -.
DR   STRING; 224325.AF_0158; -.
DR   EnsemblBacteria; AAB91076; AAB91076; AF_0158.
DR   GeneID; 24793709; -.
DR   KEGG; afu:AF_0158; -.
DR   eggNOG; arCOG02024; Archaea.
DR   HOGENOM; CLU_751463_0_0_2; -.
DR   OMA; YFAPANY; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="Tetrathionate reductase subunit C"
FT                   /id="PRO_0000417419"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   361 AA;  40083 MW;  1BA225D1C94FCF48 CRC64;
     MLWSYPEGFA YFNEFAQSII WEPVAFSYAL LISGADLLLL AALALLSGYL RRAIPMFLIL
     GLSFFSVILL GPLADLALPH RATEILTRPH LASTEMHPGI SVMALYGGLL WPLTFIVALI
     FALLYFSYPM HKKGGTFSFL SFGVKSEESY ERLKPAMKVL AAILVPLSAL WTIYPGMLFF
     SQTWIYAWKN WGLMLPMFFG ETFITATGTA LILYYLERME DERIRYPLLQ IHGAAAIALA
     GVLILQMFIW GMWGNPNFAA VVPMMQAAAV IFLLTFILTL VSAKYEAITP IVPVLALFGV
     VVNKWNLIIN GQLISRAGMG VLEPELAPNW LAEAVSPIAL AILLLVILSY IFPMEVEEDA
     A
 
 
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