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