ID Q68X98_RICTY Unreviewed; 251 AA. AC Q68X98; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 24-JAN-2024, entry version 91. DE RecName: Full=Cytochrome c1 {ECO:0000256|ARBA:ARBA00016165}; DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951}; DE AltName: Full=Complex III subunit 4 {ECO:0000256|ARBA:ARBA00041779}; DE AltName: Full=Complex III subunit IV {ECO:0000256|ARBA:ARBA00041724}; DE AltName: Full=Cytochrome b-c1 complex subunit 4 {ECO:0000256|ARBA:ARBA00041262}; DE AltName: Full=Cytochrome c1, heme protein, mitochondrial {ECO:0000256|ARBA:ARBA00040084}; GN Name=fbcH {ECO:0000313|EMBL:AAU03744.1}; GN OrderedLocusNames=RT0263 {ECO:0000313|EMBL:AAU03744.1}; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=257363 {ECO:0000313|EMBL:AAU03744.1, ECO:0000313|Proteomes:UP000000604}; RN [1] {ECO:0000313|EMBL:AAU03744.1, ECO:0000313|Proteomes:UP000000604} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington {ECO:0000313|Proteomes:UP000000604}; RX PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., RA Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with sequences RT of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). 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 c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1}; CC Note=Binds 1 heme c group covalently per subunit. CC {ECO:0000256|PIRSR:PIRSR602326-1}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004434}. 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; AE017197; AAU03744.1; -; Genomic_DNA. DR RefSeq; WP_011190729.1; NC_006142.1. DR AlphaFoldDB; Q68X98; -. DR KEGG; rty:RT0263; -. DR eggNOG; COG2857; Bacteria. DR HOGENOM; CLU_040334_1_2_5; -. DR OMA; WVKKFKW; -. DR OrthoDB; 9808471at2; -. DR Proteomes; UP000000604; Chromosome. DR GO; GO:0016020; C: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 Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR002326; Cyt_c1. DR InterPro; IPR021157; Cyt_c1_TM_anchor_C. DR PANTHER; PTHR10266; CYTOCHROME C1; 1. DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF02167; Cytochrom_C1; 1. DR PRINTS; PR00603; CYTOCHROMEC1. DR SUPFAM; SSF46626; Cytochrome c; 1. DR SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 1. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602326-1}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..251 FT /note="Cytochrome c1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004269893" FT TRANSMEM 224..242 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 44..151 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT BINDING 57 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1" FT BINDING 60 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1" FT BINDING 61 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1" FT BINDING 180 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1" SQ SEQUENCE 251 AA; 28657 MW; FCAB3390401B0D38 CRC64; MNTKLLIFII LFVTSSLSIA NTEALHLKKM KWSFDGIFGT VNREAAQRGF QVYKEVCSVC HSLNNLYYRN LKDIGFSDDE IKEIAKGYTV KDGPNDDGEM FERPALPYDR FVQPYPNEQA ARKANNGANP PDLSLIIKAR YDGANYIYSL LTSYTDPPAY FKMMHGAHYN PYFPGAQIVM PPPLTDGQVT YMDGTNASVE QMSRDVTVFL QWAAEPEMEH RKSIGLKVMM FLIVFTILFY IAKNRIWSNL K //