ID Q5FG01_EHRRG Unreviewed; 174 AA.
AC Q5FG01;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Cytochrome c homolog {ECO:0000256|ARBA:ARBA00015074};
GN Name=cycM {ECO:0000313|EMBL:CAI28149.1};
GN OrderedLocusNames=ERGA_CDS_06970 {ECO:0000313|EMBL:CAI28149.1};
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI28149.1, ECO:0000313|Proteomes:UP000000533};
RN [1] {ECO:0000313|EMBL:CAI28149.1, ECO:0000313|Proteomes:UP000000533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel {ECO:0000313|EMBL:CAI28149.1,
RC ECO:0000313|Proteomes:UP000000533};
RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
CC -!- FUNCTION: May be involved in electron transfer from bc1 complex to aa3.
CC {ECO:0000256|ARBA:ARBA00002071}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the cytochrome c family.
CC {ECO:0000256|ARBA:ARBA00006488}.
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DR EMBL; CR925677; CAI28149.1; -; Genomic_DNA.
DR RefSeq; WP_011255781.1; NC_006831.1.
DR AlphaFoldDB; Q5FG01; -.
DR KEGG; erg:ERGA_CDS_06970; -.
DR HOGENOM; CLU_060944_4_0_5; -.
DR OrthoDB; 9805828at2; -.
DR Proteomes; UP000000533; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..174
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 174 AA; 19265 MW; 63A70745F0BB24B5 CRC64;
MDGFQLNKIF TAILFACFIV LFVSNVTDLL YNPEPHAEPV RGYKVDVEQQ GLIEESAAVP
DVQVDIQALV AQANITKGKE ISKKCVSCHT FEKGGANKVG PNLWHIIGNK KAHLGDAFNY
SKAMLNIGGT WEYHDLFQFL TKPQAYVKGT RMAFAGISKP QDIADLIAYM KSLE
//
