HMEB_ARCFU
ID HMEB_ARCFU Reviewed; 395 AA.
AC O29750;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Hdr-like menaquinol oxidoreductase integral membrane subunit;
DE Short=Hme subunit B;
GN Name=hmeB; OrderedLocusNames=AF_0500;
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 DISCUSSION OF SEQUENCE.
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. HmeB subunit may function
CC as a menaquinol-oxidizing site. HmeA, HmeB and HmeE subunits may
CC together catalyze electron transfer from menaquinol to cytochrome c.
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}.
CC -!- SIMILARITY: Belongs to the NrfD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB90737.1; -; Genomic_DNA.
DR PIR; D69312; D69312.
DR RefSeq; WP_010878007.1; NC_000917.1.
DR AlphaFoldDB; O29750; -.
DR SMR; O29750; -.
DR STRING; 224325.AF_0500; -.
DR EnsemblBacteria; AAB90737; AAB90737; AF_0500.
DR GeneID; 24794040; -.
DR KEGG; afu:AF_0500; -.
DR eggNOG; arCOG02025; Archaea.
DR HOGENOM; CLU_045348_3_1_2; -.
DR OMA; WNASILA; -.
DR OrthoDB; 101534at2157; -.
DR PhylomeDB; O29750; -.
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; IPR005614; NrfD_fam.
DR Pfam; PF03916; NrfD; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..395
FT /note="Hdr-like menaquinol oxidoreductase integral membrane
FT subunit"
FT /id="PRO_0000159324"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 44195 MW; B8622ADFC9EB9F23 CRC64;
MAVEFKKIEG DSIQYFALVI ILAAVTALGF YAYVLDHKMG LNGLSNRVPW GIVNAGIPYF
IGLSAGSLIV SALAGVFNIK KYKVFSRIAA YMAAAWIIAA ILSIALDIGK LYHFMNAVRY
FNPTSIFSWN AFLYSSYFVI CSIYLLVQFE EMEKATRFMA GLAVFWAVLV HSGTGAIYSF
VYSKELYHSA LTPPMFIVCA ITSGLGLLLA NLYFTFRFTK RELDPKLIRG LALIFAGLMM
VLGYFLAVEG LEKGYIPALH EAVQFVFLTP TSGVFWSFWL LVIFGIAIPI IIVLNPKTGY
DLRWITFAGI LHAALVFAER FYLIIPGQVF PEEYLPGYEL ESLHTLEGYI VSYTPSVFEW
LQVIGLIAMV YLIFVVGVKL FALIPERAVE EVVEE