ID CYCM_RICBR Reviewed; 173 AA. AC Q1RHX7; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=Cytochrome c homolog; GN Name=cycM; OrderedLocusNames=RBE_0956; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RML369-C; RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in RT gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:733-744(2006). CC -!- FUNCTION: May be involved in electron transfer from bc1 complex to aa3. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II CC membrane protein {ECO:0000250}. CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}. 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; CP000087; ABE05037.1; -; Genomic_DNA. DR RefSeq; WP_011477618.1; NC_007940.1. DR AlphaFoldDB; Q1RHX7; -. DR SMR; Q1RHX7; -. DR KEGG; rbe:RBE_0956; -. DR eggNOG; COG3474; Bacteria. DR HOGENOM; CLU_060944_4_0_5; -. DR OrthoDB; 9805828at2; -. DR Proteomes; UP000001951; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR002327; Cyt_c_1A/1B. DR PANTHER; PTHR11961; CYTOCHROME C; 1. DR PANTHER; PTHR11961:SF56; CYTOCHROME C-1; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; Cytochrome c; 1. DR PROSITE; PS51007; CYTC; 1. PE 3: Inferred from homology; KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..173 FT /note="Cytochrome c homolog" FT /id="PRO_0000288755" FT TOPO_DOM 1..8 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 9..29 FT /note="Helical; Signal-anchor" FT /evidence="ECO:0000255" FT TOPO_DOM 30..173 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT BINDING 82 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 85 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 86 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 148 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" SQ SEQUENCE 173 AA; 18831 MW; E7BB19C8EFADCF72 CRC64; MSGKELNKIV AAILFASLIA MMVGFIANIL YKPVLEPKHR GYSIAVQEVS EAPTTQAQAP INIPELMKTA NADNGREIAK KCLMCHSLDK DGPNKIGPHL WDVAGRPKAS ITDYKYSPAL SALGGNWDDD SLFAFLHKPS SYAPGTKMSF AGISKPQDIA DVILFLKTYV HDK //