ID A9M091_NEIM0 Unreviewed; 193 AA.
AC A9M091;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00019816, ECO:0000256|RuleBase:RU004494};
DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951, ECO:0000256|RuleBase:RU004494};
GN Name=petA {ECO:0000313|EMBL:ABX72352.1};
GN OrderedLocusNames=NMCC_0133 {ECO:0000313|EMBL:ABX72352.1};
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833 {ECO:0000313|EMBL:ABX72352.1, ECO:0000313|Proteomes:UP000001177};
RN [1] {ECO:0000313|EMBL:ABX72352.1, ECO:0000313|Proteomes:UP000001177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442 {ECO:0000313|EMBL:ABX72352.1,
RC ECO:0000313|Proteomes:UP000001177};
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000256|ARBA:ARBA00002444}.
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|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|ARBA:ARBA00011649,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000381; ABX72352.1; -; Genomic_DNA.
DR RefSeq; WP_002215005.1; NC_010120.1.
DR AlphaFoldDB; A9M091; -.
DR GeneID; 66754082; -.
DR KEGG; nmn:NMCC_0133; -.
DR HOGENOM; CLU_055690_0_2_4; -.
DR Proteomes; UP000001177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.20.5.510; Single helix bin; 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; IPR019470; Ubiq_cytC_Rdtase_Fe-S_su_TAT.
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 Pfam; PF10399; UCR_Fe-S_N; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004494"
FT DOMAIN 85..189
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 193 AA; 20632 MW; 1A61E1171860EBDC CRC64;
MDNQEINNGR RRFLTLATCG AGGVAALGVA TPFVASFFPS EKAKAAGAAV EVDVSKIEAG
QLLTAEWQGK PIWVLNRTDQ QLKDLKGLNG ELTDPNSDAE QQPEYAKNET RSIKPNILVA
IGICTHLGCS PTFRPDIAPA DLGADWKGGF FCPCHGSKFD LAGRVYKGVP APTNLVVPPY
KYLSDTTILV GED
//
