ID V6JZ08_STRNV Unreviewed; 258 AA.
AC V6JZ08;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=M877_31150 {ECO:0000313|EMBL:EST21929.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST21929.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST21929.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST21929.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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:EST21929.1}.
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DR EMBL; AWQW01000225; EST21929.1; -; Genomic_DNA.
DR AlphaFoldDB; V6JZ08; -.
DR STRING; 193462.BBN63_25860; -.
DR PATRIC; fig|1352941.4.peg.6329; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_086567_0_0_11; -.
DR Proteomes; UP000017971; Chromosome.
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:EST21929.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR000007};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000007};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..258
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039418049"
FT TRANSMEM 231..250
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR000007"
FT DOMAIN 36..115
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 131..209
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 49
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 52
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 53
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 144
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 147
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 148
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 258 AA; 26079 MW; 78477EDADC77504E CRC64;
MAAVVVLLLA LAATGGLYAA FAPAGKAQAD DTAQSLAIDE GKKLYAVGCA SCHGVGGQGT
TDGPSLTGVG AAAVDFQVGT GRMPAQQPGP QVPKKKVIYD QKEIDQLAAY VASLGPGPSV
PTAGQYNPQG ADAAKGGELF RSNCAQCHNF GGEGGALTNG KYAPGLEGVT PKHLYEAMLT
GPQNMPAFPD STMPEQQKQD IIKYIESVNS STSANPGGLK LGGIGPVSEG LFSWIIGLGA
LVAVAVWVAA HTAKARKS
//
