ID H6RCY7_NOCCG Unreviewed; 546 AA. AC H6RCY7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 04-NOV-2026, entry version 58. DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00016116}; DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951}; DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB {ECO:0000256|ARBA:ARBA00029568}; GN Name=qcrB {ECO:0000313|EMBL:CCF62631.1}; GN OrderedLocusNames=NOCYR_1845 {ECO:0000313|EMBL:CCF62631.1}; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Nocardiaceae; Nocardia. OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF62631.1, ECO:0000313|Proteomes:UP000008190}; RN [1] {ECO:0000313|EMBL:CCF62631.1, ECO:0000313|Proteomes:UP000008190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF62631.1, RC ECO:0000313|Proteomes:UP000008190}; RX PubMed=22461543; DOI=10.1128/JB.00161-12; RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L., RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S., RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V., RA Richard Y., Cournoyer B., Blaha D.; RT "Genome sequence of the human- and animal-pathogenic strain Nocardia RT cyriacigeorgica GUH-2."; RL J. Bacteriol. 194:2098-2099(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|ARBA:ARBA00029351}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000256|PROSITE- CC ProRule:PRU00968}. 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; FO082843; CCF62631.1; -; Genomic_DNA. DR RefSeq; WP_014350096.1; NC_016887.1. DR AlphaFoldDB; H6RCY7; -. DR STRING; 1127134.NOCYR_1845; -. DR KEGG; ncy:NOCYR_1845; -. DR eggNOG; COG1290; Bacteria. DR HOGENOM; CLU_031114_2_0_11; -. DR OMA; AAAMFHM; -. DR OrthoDB; 9804503at2; -. DR Proteomes; UP000008190; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008121; F:quinol-cytochrome-c reductase activity; IEA:UniProtKB-EC. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR FunFam; 1.20.810.10:FF:000007; Ubiquinol-cytochrome C reductase B subunit; 1. DR Gene3D; 1.20.810.10; Cytochrome Bc1 Complex, Chain C; 1. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR016174; Di-haem_cyt_TM. DR NCBIfam; NF050120; bc1_QcrB_actin; 1. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF13631; Cytochrom_B_N_2; 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|PROSITE- KW ProRule:PRU00968}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00968}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00968}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE- KW ProRule:PRU00968}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00968}; Reference proteome {ECO:0000313|Proteomes:UP000008190}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE- KW ProRule:PRU00968}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00968}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE- KW ProRule:PRU00968}. FT TRANSMEM 40..66 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 110..131 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 209..234 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 331..352 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 372..391 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 411..432 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 14..241 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT BINDING 111 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00968" FT BINDING 125 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00968" FT BINDING 213 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00968" FT BINDING 228 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00968" SQ SEQUENCE 546 AA; 60670 MW; 120A52026520F0E7 CRC64; MSSPSAIGRK VGAHADAVDE RYRAAAFMRR SINKVFPTHW SFLLGEIALY AFIILLLSGV YLTLYFDPSM SHVVYDGAYQ PLRGVGMSRA YETALNISFE VRGGLFVRQV HHWAALLFAA SIIVHLLRIF FTGAFRKPRE ANWVIGSLLL ILAMFEGFFG YSLPDDLLSG TGLRAAFSGI TIGVPVIGTW LHWLMFGGDF PGEIIIPRLY IAHVLLFPGI MLALIAAHVA IVWYQKHTQF PGPGRTENNV VGARIVPVFA ADQGAFFAFT LGFVGIMGGV LQINPIWNLG PYNPSQVSAG SQPDFYMMWT DGMARLMPPW ELYLGRYTVP AVFWVALVMG LVFTLLIAYP WIEKRLTKDN ANHNLLQRPR DVPVRTAIGA MAITFYVILT LACVNDIISL KFDISLNATT WVGRIGLLLG PPIAYFLTYR FCIGLQRSDR AVLEHGIETG VIKRLPHGEY IEVHQPLGPV DDHGHPIPLE YQGAPVPKKM NQLGSAGQPG TGSFLRPDPW QESEQHFATE LEEEHKQLAV LRKAQENANG HGKHSH //