CYCM_RICPR
ID CYCM_RICPR Reviewed; 175 AA.
AC Q9ZDS2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome c homolog;
GN Name=cycM; OrderedLocusNames=RP253;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
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DR EMBL; AJ235271; CAA14715.1; -; Genomic_DNA.
DR PIR; A71680; A71680.
DR RefSeq; NP_220638.1; NC_000963.1.
DR RefSeq; WP_004598522.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDS2; -.
DR SMR; Q9ZDS2; -.
DR STRING; 272947.RP253; -.
DR EnsemblBacteria; CAA14715; CAA14715; CAA14715.
DR GeneID; 57569381; -.
DR KEGG; rpr:RP253; -.
DR PATRIC; fig|272947.5.peg.260; -.
DR eggNOG; COG3474; Bacteria.
DR HOGENOM; CLU_060944_4_0_5; -.
DR OMA; KGYIPGT; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 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..175
FT /note="Cytochrome c homolog"
FT /id="PRO_0000288758"
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..175
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 87
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 88
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 150
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 175 AA; 19286 MW; 5E3422344225017D CRC64;
MTGKELNKIV AAILFASLIA MIVGFIANIL YKPNLHVLHR GYSIAIQKSS SNESATVIAQ
ESVNIQELMK TANANHGREI AKKCLMCHSL DKDGPNKLGP HLWNIVGRPK ASITDYKYSF
AISKLGGVWD DENLFAFLHK PSSYAPGTKM SFAGISKPQD IADVILFLKN YVHDQ
