HMEC_ARCFU
ID HMEC_ARCFU Reviewed; 332 AA.
AC O29749;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Hdr-like menaquinol oxidoreductase cytochrome b-like subunit;
DE Short=Hme subunit C;
GN Name=hmeC; OrderedLocusNames=AF_0501;
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 PROTEIN SEQUENCE OF 1-15.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=11952791; DOI=10.1046/j.1432-1033.2002.02839.x;
RA Mander G.J., Duin E.C., Linder D., Stetter K.O., Hedderich R.;
RT "Purification and characterization of a membrane-bound enzyme complex from
RT the sulfate-reducing archaeon Archaeoglobus fulgidus related to
RT heterodisulfide reductase from methanogenic archaea.";
RL Eur. J. Biochem. 269:1895-1904(2002).
CC -!- FUNCTION: Has menaquinol-oxidizing activity. HmeC and HmeD subunits may
CC together mediate electron transfer from menaquinol to an unidentified
CC electron acceptor on the cytoplasmic side of the membrane.
CC -!- SUBUNIT: Consists of five subunits: an integral membrane subunit, a
CC cytochrome b-like subunit, a cytochrome c subunit and two iron-sulfur
CC subunits.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE000782; AAB90736.1; -; Genomic_DNA.
DR PIR; E69312; E69312.
DR RefSeq; WP_010878008.1; NC_000917.1.
DR AlphaFoldDB; O29749; -.
DR STRING; 224325.AF_0501; -.
DR PRIDE; O29749; -.
DR EnsemblBacteria; AAB90736; AAB90736; AF_0501.
DR GeneID; 24794041; -.
DR KEGG; afu:AF_0501; -.
DR eggNOG; arCOG02194; Archaea.
DR HOGENOM; CLU_067516_0_0_2; -.
DR OMA; IPTTCGQ; -.
DR OrthoDB; 88021at2157; -.
DR PhylomeDB; O29749; -.
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.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..332
FT /note="Hdr-like menaquinol oxidoreductase cytochrome b-like
FT subunit"
FT /id="PRO_0000084006"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 11
FT /note="P -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38386 MW; A5A4E82663469651 CRC64;
MIGVIFGVIV PYIAVAIFVI GVIYRIVNWA NSAVPLKIPT TGGQQKSFPF IKRTIYDRFD
SPYTWWETAG RMLLEIFFFR SLLKNTRYYL DRVSQKDARW LWLFGILFHY SLLLVLIRHS
RFFLDPVPSF VETLSEIEAF KGVFIPSVYM SGLAIVAALF LLWLRRIFLS RERTLSLPSD
HFALILLLAI TISGNVMRYF VKADLFAVKE LLMSLMTFNI GHAVEVANTI EPIFYVHFAL
ASFLLAYFPF SKLMHAGGVF FSPTRNMPND NRARRHVNPW DPADVPLLAK GITVAGRVYK
SKKLDWDTYY SMYTDQLQEI EEADYKIVPE EL