ID A0A0K9H6K9_9BACI Unreviewed; 255 AA.
AC A0A0K9H6K9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Menaquinol:cytochrome c reductase cytochrome c subunit {ECO:0000256|PIRNR:PIRNR036636};
GN ORFNames=AC623_12280 {ECO:0000313|EMBL:KMY54604.1};
OS Bacillus sp. FJAT-27231.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY54604.1, ECO:0000313|Proteomes:UP000037077};
RN [1] {ECO:0000313|Proteomes:UP000037077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMY54604.1}.
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DR EMBL; LFZU01000001; KMY54604.1; -; Genomic_DNA.
DR RefSeq; WP_049662879.1; NZ_LFZU01000001.1.
DR AlphaFoldDB; A0A0K9H6K9; -.
DR STRING; 1679168.AC623_12280; -.
DR PATRIC; fig|1679168.3.peg.2630; -.
DR OrthoDB; 2380469at2; -.
DR Proteomes; UP000037077; Unassembled WGS sequence.
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:UP000037077};
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..255
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
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 197
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036636-50"
FT BINDING 198
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 255 AA; 28288 MW; A74A556FC759DF46 CRC64;
MHRGKGMKFV GDSRIPAVRK PNVPKDYSEY PGKTEAFWPN FLLKEWMVGA VFLVGYLCLT
VAHPSPLERV ADPTDTGYIP LPDWYFLFLY QLLKYTYASG PYNVIGAFVI PGLAFGGLLL
APFIDRGPER RPIKRPFATG FMLLALAATI FLTWESVIHH DWEAAEAQGK IVEEADFDKN
DEGYKIFADQ KNGCINCHGE NLTGGAAAPS LVGTGLKPEE IKKIAHEGKG AMPPNMFKGT
DEELDKMAEF ISNLK
//
