ID CYB_RICCN Reviewed; 398 AA. AC Q92IR1; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Cytochrome b; GN Name=petB; Synonyms=cytB; OrderedLocusNames=RC0359; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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:0000250}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; CC Note=Binds 2 heme b groups non-covalently. {ECO:0000250}; CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs CC at about 566 nm. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE- CC ProRule:PRU00967, ECO:0000255|PROSITE-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; AE006914; AAL02897.1; -; Genomic_DNA. DR PIR; G97744; G97744. DR RefSeq; WP_010977014.1; NC_003103.1. DR AlphaFoldDB; Q92IR1; -. DR SMR; Q92IR1; -. DR GeneID; 928546; -. DR KEGG; rco:RC0359; -. DR PATRIC; fig|272944.4.peg.408; -. DR HOGENOM; CLU_031114_3_0_5; -. DR Proteomes; UP000000816; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Respiratory chain; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..398 FT /note="Cytochrome b" FT /id="PRO_0000280934" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 192..212 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 245..265 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 277..297 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 95 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 109 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 196 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 210 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" SQ SEQUENCE 398 AA; 45829 MW; 148A8A349574B7BF CRC64; MNEDITPKKP NAIIEWIDYR LPIFAFLKHF SHYQTPKNLN YLWNLGSIAG IALVIQIITG VILAMHYTPH VDHAFDSVER IMRNVNYGWL LRYTHAVGAS MFFAAVYLHI ARGLYYGSYK APRELLWHIG IIIFLTMMAT AFMGYVLPWG QMSYWGATVI TNLFSAIPLI GEFIVTWLWG GFSVDNPTLN RFFSLHYLLP FIIVALVMLH LVALHQHGSN NPKGIDVKSP KDTIPFHPYY TVKDFVGFGV YFIIFAYFIF YEPNYLGHPD NYIPANPLVT PAHIVPEWYF LPFYAILRAM PSKLGGVLLM FGSIFVLFLL PWLDTSKVRS SNYRPIYRMA FWIFMADCLL LGYLGGQPAE EPYITISRFA ACYYFFHVLV ALPLIGKYEK PLPLPEEL //