ID   CYBH_RHOCA              Reviewed;         262 AA.
AC   P16145;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Probable Ni/Fe-hydrogenase B-type cytochrome subunit;
GN   Name=hupC; Synonyms=hupM;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=2094292; DOI=10.1016/0378-1097(90)90488-c;
RA   Richaud P., Vignais P.M., Colbeau A., Uffen R.L., Cauvin B.;
RT   "Molecular biology studies of the uptake hydrogenase of Rhodobacter
RT   capsulatus and Rhodocyclus gelatinosus.";
RL   FEMS Microbiol. Rev. 7:413-418(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=3067084; DOI=10.1007/bf00340186;
RA   Leclerc M., Colbeau A., Cauvin B., Vignais P.M.;
RT   "Cloning and sequencing of the genes encoding the large and the small
RT   subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus.";
RL   Mol. Gen. Genet. 214:97-107(1988).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1791762; DOI=10.1111/j.1365-2958.1991.tb02098.x;
RA   Cauvin B., Colbeau A., Vignais P.M.;
RT   "The hydrogenase structural operon in Rhodobacter capsulatus contains a
RT   third gene, hupM, necessary for the formation of a physiologically
RT   competent hydrogenase.";
RL   Mol. Microbiol. 5:2519-2527(1991).
CC   -!- FUNCTION: Probable b-type cytochrome.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the HupC/HyaC/HydC family. {ECO:0000305}.
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DR   EMBL; X13520; CAA31871.1; -; Genomic_DNA.
DR   AlphaFoldDB; P16145; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   InterPro; IPR000516; Ni-dep_Hydgase_cyt-B.
DR   Pfam; PF01292; Ni_hydr_CYTB; 1.
DR   PRINTS; PR00161; NIHGNASECYTB.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   TIGRFAMs; TIGR02125; CytB-hydogenase; 1.
DR   PROSITE; PS00882; NI_HGENASE_CYTB_1; 1.
DR   PROSITE; PS00883; NI_HGENASE_CYTB_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..262
FT                   /note="Probable Ni/Fe-hydrogenase B-type cytochrome
FT                   subunit"
FT                   /id="PRO_0000201383"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   262 AA;  30215 MW;  244D7E9CD6DBF4C1 CRC64;
     MKGVSDERIN APVRGPDEIF EASRLTGDAT REDLESIRRR TSVYVYEAPV RVWHWVNALA
     ITILVVTGYF IASPLPSMQI GEATDQFVMG YIRFAHFAAG VVMSVAFFGR IYWAFVGNRH
     AWQMFYIPIF NKRYWKEFVF ELRWYFFLEE EPKKYIGHNP LAHAAMFTFI TLGITFMMIT
     GWALYAEGAG QGGVTDSLFG WVLGYVQNSQ RLHTLHHLGM WAIVIFAIIH IYAAVREDVM
     SRQSMVSTMI SGHRTFKDDR IE