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Database: UniProt
Entry: A0A1Q2CD58_9ACTN
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ID   A0A1Q2CD58_9ACTN        Unreviewed;       269 AA.
AC   A0A1Q2CD58;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=RPIT_03715 {ECO:0000313|EMBL:AQP44031.1}, SAMN05428934_101345
GN   {ECO:0000313|EMBL:SDY32659.1};
OS   Tessaracoccus flavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP44031.1, ECO:0000313|Proteomes:UP000188324};
RN   [1] {ECO:0000313|EMBL:AQP44031.1, ECO:0000313|Proteomes:UP000188324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP44031.1,
RC   ECO:0000313|Proteomes:UP000188324};
RX   PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA   Kumari R., Singh P., Schumann P., Lal R.;
RT   "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT   lindane-producing factory.";
RL   Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN   [2] {ECO:0000313|EMBL:SDY32659.1, ECO:0000313|Proteomes:UP000199635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1 {ECO:0000313|EMBL:SDY32659.1,
RC   ECO:0000313|Proteomes:UP000199635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQP44031.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP44031.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP019605; AQP44031.1; -; Genomic_DNA.
DR   EMBL; FNPU01000001; SDY32659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2CD58; -.
DR   STRING; 1610493.RPIT_03715; -.
DR   KEGG; tfl:RPIT_03715; -.
DR   Proteomes; UP000188324; Chromosome.
DR   Proteomes; UP000199635; 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:SF9; CYTOCHROME C4; 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|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:AQP44031.1};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000007};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188324};
KW   Respiratory chain {ECO:0000256|PIRNR:PIRNR000007};
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|PIRNR:PIRNR000007}.
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR000007"
FT   DOMAIN          45..124
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         58
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         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         62
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   269 AA;  27982 MW;  1BBF3BE1DDE600B7 CRC64;
     MQIFSTLRRH GAARPLLLIL ALLLVGLSYS AVSPQRSSAE TEMTQQIEEG KALFDFTCSS
     CHGLGGEGTS QGPSLIGVGA ASVDFQMGTG RMPAARQEAQ LPARKVNYTQ EQIEAVAAYV
     ATLGPGPGIP AESAYTLSLE GDEKAEAIAR GGALFRANCS ACHGIVGGGG AMPNGKFAPS
     LAETSDVHIY EAVRTGPQQM PLFSKEVMPD ESVAEIIAYL NGAEEQANYG GITMGDAGPV
     SEGFWAFIIG IGGFALIATW IAKKGARAR
//
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