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Database: UniProt
Entry: A0A2N5MKK3_9BACI
LinkDB: A0A2N5MKK3_9BACI
Original site: A0A2N5MKK3_9BACI 
ID   A0A2N5MKK3_9BACI        Unreviewed;       253 AA.
AC   A0A2N5MKK3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Menaquinol:cytochrome c reductase cytochrome c subunit {ECO:0000256|PIRNR:PIRNR036636};
GN   ORFNames=CUU64_05645 {ECO:0000313|EMBL:PLT34886.1};
OS   Bacillus sp. V5-8f.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053044 {ECO:0000313|EMBL:PLT34886.1, ECO:0000313|Proteomes:UP000235260};
RN   [1] {ECO:0000313|EMBL:PLT34886.1, ECO:0000313|Proteomes:UP000235260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V5-8f {ECO:0000313|EMBL:PLT34886.1,
RC   ECO:0000313|Proteomes:UP000235260};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant Strains Isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) 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:PLT34886.1}.
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DR   EMBL; PGUW01000004; PLT34886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5MKK3; -.
DR   OrthoDB; 2380469at2; -.
DR   Proteomes; UP000235260; 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:UP000235260};
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..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..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..251
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
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   253 AA;  27720 MW;  4EF4466356E55DC4 CRC64;
     MHRGKGMKFV GDSRVPAARK PNIPKDYSEY PGKTEAFWPN FLLKEWMVGA VFLIGYLCLT
     VAHPSPLEKI ADPTDTAYIP LPDWYFLFLY QLLKYTYASG PYNVIGALVI PGLAFGALLL
     APFIDRGPQR RPSKRPFATG FMLLAVAAVF YLTWQSVVTH DWEAAKKQGQ IVAESSVDKE
     SDGYKHYKAS CAGCHGNELS GGTGPKLLDT GLAPEEVAKI AREGKGAMPP GVFKGSDEEL
     KVLAEFISNA KTE
//
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