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Database: UniProt
Entry: K0MBG1_BORPB
LinkDB: K0MBG1_BORPB
Original site: K0MBG1_BORPB 
ID   K0MBG1_BORPB            Unreviewed;       213 AA.
AC   K0MBG1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit {ECO:0000256|RuleBase:RU004494};
DE            EC=7.1.1.8 {ECO:0000256|RuleBase:RU004494};
GN   Name=petA {ECO:0000313|EMBL:CCJ51749.1};
GN   OrderedLocusNames=BN117_4416 {ECO:0000313|EMBL:CCJ51749.1};
OS   Bordetella parapertussis (strain Bpp5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ51749.1, ECO:0000313|Proteomes:UP000008035};
RN   [1] {ECO:0000313|EMBL:CCJ51749.1, ECO:0000313|Proteomes:UP000008035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ51749.1,
RC   ECO:0000313|Proteomes:UP000008035};
RX   PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA   Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA   Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT   "Comparative genomics of the classical Bordetella subspecies: the evolution
RT   and exchange of virulence-associated diversity amongst closely related
RT   pathogens.";
RL   BMC Genomics 13:545-545(2012).
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|RuleBase:RU004494};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU004494};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU004494};
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein. {ECO:0000256|RuleBase:RU004497}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC       {ECO:0000256|RuleBase:RU004494}.
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DR   EMBL; HE965803; CCJ51749.1; -; Genomic_DNA.
DR   RefSeq; WP_003815815.1; NC_018828.1.
DR   RefSeq; YP_006898132.1; NC_018828.1.
DR   AlphaFoldDB; K0MBG1; -.
DR   GeneID; 69603469; -.
DR   KEGG; bpar:BN117_4416; -.
DR   HOGENOM; CLU_055690_0_2_4; -.
DR   Proteomes; UP000008035; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   NCBIfam; TIGR01416; Rieske_proteo; 1.
DR   PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|RuleBase:RU004494};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004494};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:CCJ51749.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004494};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004494}; Transport {ECO:0000256|RuleBase:RU004494}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004494"
FT   DOMAIN          103..204
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  22850 MW;  D7BCFDCC6281FE36 CRC64;
     MSQDTLVHDD DGAVDPNLPP DPSRRFWVTT ACAVGGVAGV ATAVPFVSTF APSEKARAAG
     APVEVDVGDL APGQMRTVEW RGKPVWIIRR TDDQLKGIKS QDGLMADPNS ERPGFTPAYA
     KNEYRSRKPE LFVCVGICTH LGCSPTAHFE TGGGAGMPGN WQGGFLCPCH GSTFDMAGRV
     YKDKPAPDNL EVPPYQYLSD TRIIVGVDED NKA
//
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