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Database: UniProt/TrEMBL
Entry: E4PNJ1_MARAH
LinkDB: E4PNJ1_MARAH
Original site: E4PNJ1_MARAH 
ID   E4PNJ1_MARAH            Unreviewed;       197 AA.
AC   E4PNJ1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 70.
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:ADP96309.1};
GN   OrderedLocusNames=HP15_545 {ECO:0000313|EMBL:ADP96309.1};
OS   Marinobacter adhaerens (strain DSM 23420 / HP15).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP96309.1, ECO:0000313|Proteomes:UP000007077};
RN   [1] {ECO:0000313|EMBL:ADP96309.1, ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX   PubMed=21304739;
RA   Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA   Glockner F.O., Grossart H.P., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT   diatom-interacting marine microorganism.";
RL   Stand. Genomic Sci. 3:97-107(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA   Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA   Gloeckner F.O., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001978; ADP96309.1; -; Genomic_DNA.
DR   RefSeq; WP_014576088.1; NC_017506.1.
DR   AlphaFoldDB; E4PNJ1; -.
DR   STRING; 225937.HP15_545; -.
DR   GeneID; 78559149; -.
DR   KEGG; mad:HP15_545; -.
DR   PATRIC; fig|225937.3.peg.552; -.
DR   eggNOG; COG0723; Bacteria.
DR   HOGENOM; CLU_055690_0_2_6; -.
DR   OMA; KRTWLIA; -.
DR   Proteomes; UP000007077; 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   Oxidoreductase {ECO:0000313|EMBL:ADP96309.1};
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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004494"
FT   DOMAIN          109..189
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   197 AA;  21277 MW;  0FEC193B03AA63EE CRC64;
     MSNGDVSQGR RRFLIGATSV VGGVGVVGAA VPFLGSWNPS AKAEAAGAPV TVNISKIEPG
     QQITVEWRGK PVWIIRRTEE MRANIEKLND RVKDPQSEAP QQPPYIDGIL RSLKPEFAVL
     VGLCTHLGCV PSYRPEVAPA DLGDEWLGGL FCPCHGSRYD MAGRVFEAQP APLNLEVPPY
     RYDDDVTLTI GLDPEAA
//
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