ID A0A221MD35_9BACI Unreviewed; 256 AA.
AC A0A221MD35;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Menaquinol:cytochrome c reductase cytochrome c subunit {ECO:0000256|PIRNR:PIRNR036636};
GN ORFNames=CFK40_11105 {ECO:0000313|EMBL:ASN05520.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN05520.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN05520.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN05520.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC -!- FUNCTION: Component of the menaquinol:cytochrome c reductase complex.
CC {ECO:0000256|PIRNR:PIRNR036636}.
CC -!- SUBUNIT: The main subunits of the menaquinol:cytochrome c complex are a
CC Rieske-type iron-sulfur protein (QcrA), a cytochrome b (QcrB) and a
CC cytochrome c (QcrC). {ECO:0000256|PIRNR:PIRNR036636}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|PIRNR:PIRNR036636}.
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DR EMBL; CP022437; ASN05520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221MD35; -.
DR KEGG; vne:CFK40_11105; -.
DR OrthoDB; 2380469at2; -.
DR Proteomes; UP000204391; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR012049; MenaQ_cyt_c_Rdtase_cyt_b/c-su.
DR PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF036636; QcrC; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR036636};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR036636-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036636-51};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036636-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR036636}.
FT TRANSMEM 46..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..154
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT DOMAIN 178..252
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036636-50"
FT BINDING 194
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036636-50"
FT BINDING 195
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR036636-51"
SQ SEQUENCE 256 AA; 28089 MW; 8EA7FB99DEA467FC CRC64;
MHKGKGMKFV GDSRISSDRK PNMPKDYSEY PGRTEAFWPN FLLKEWLVGA VFLVGFLCLV
LAHPSPLEGV ADPTNATYIP LPDWYFLFLY ELLKYDFASG PYTLFGIIIL PGLAFGGLLL
APFLDRGPGR RPHQRPIAVA MMVLGLASVM LLTWESASHV DWEARAEANK PVPTTEIDKE
NPGYAVFESN CMTCHGDSLQ GGAAAPSLIG IDYSKEEIMK IAQEGIGTMP AGVFKGTDKE
LEALAEFIVS VNEEAK
//
