ID A0A1U7MNR2_9MICO Unreviewed; 267 AA.
AC A0A1U7MNR2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytochrome bc1 complex cytochrome c subunit {ECO:0000256|ARBA:ARBA00017819, ECO:0000256|PIRNR:PIRNR000007};
DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951, ECO:0000256|PIRNR:PIRNR000007};
GN ORFNames=BJF81_06520 {ECO:0000313|EMBL:OLT20039.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT20039.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT20039.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT20039.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00029351,
CC ECO:0000256|PIRNR:PIRNR000007};
CC -!- SUBUNIT: The cytochrome bc1 complex is composed of a cytochrome b
CC (QcrB), the Rieske iron-sulfur protein (QcrA) and a diheme cytochrome c
CC (QcrC) subunit. {ECO:0000256|PIRNR:PIRNR000007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|PIRNR:PIRNR000007}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR000007}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000007-50}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PIRNR:PIRNR000007}.
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:OLT20039.1}.
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DR EMBL; MKKA01000059; OLT20039.1; -; Genomic_DNA.
DR RefSeq; WP_075958906.1; NZ_MKKA01000059.1.
DR AlphaFoldDB; A0A1U7MNR2; -.
DR STRING; 1904966.BJF81_06520; -.
DR OrthoDB; 9811281at2; -.
DR Proteomes; UP000185694; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR009152; bc1_cytC-su.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR PANTHER; PTHR33751:SF13; CYTOCHROME BC1 COMPLEX CYTOCHROME C SUBUNIT; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000007; Ubiq_cycred_cyc; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000007};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000007};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000007};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000007};
KW Lyase {ECO:0000313|EMBL:OLT20039.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR000007};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000007};
KW Reference proteome {ECO:0000313|Proteomes:UP000185694};
KW Respiratory chain {ECO:0000256|PIRNR:PIRNR000007};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000007};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR000007};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR000007};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000007}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..267
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012662599"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR000007"
FT DOMAIN 48..130
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 146..224
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 61
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 65
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-51"
FT BINDING 159
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 162
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 163
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-51"
SQ SEQUENCE 267 AA; 27349 MW; CEDB7C18AD956198 CRC64;
MSSLAARRRS PLALLVLLLL GLTFTGTAYA AFAPKAAPGT SAATATQEDV EAGEQLFLAN
CATCHGTNAQ GVDPIGPSLI GVGAASVDFQ VSTGRMPLPA PGVQAERNAA QVQFSEEQIS
QLAAYVDSLG PGPDVPDEEY LDLEGADIAA GGAAYRTNCA MCHNSSGTGG ALTRGKYAPT
LMGVEPQHIY EAMLTGPQSM PVFNDQNLTP QEKENVIAFL KYIEDGGNSH GGAGLGSVGP
AGDALFVWTI GIGVMIAAAI WIGRKAA
//
