CCME_EHRRG
ID CCME_EHRRG Reviewed; 134 AA.
AC Q5FHG0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cytochrome c-type biogenesis protein CcmE {ECO:0000255|HAMAP-Rule:MF_01959};
DE AltName: Full=Cytochrome c maturation protein E {ECO:0000255|HAMAP-Rule:MF_01959};
DE AltName: Full=Heme chaperone CcmE {ECO:0000255|HAMAP-Rule:MF_01959};
GN Name=ccmE {ECO:0000255|HAMAP-Rule:MF_01959};
GN Synonyms=cycJ {ECO:0000255|HAMAP-Rule:MF_01959};
GN OrderedLocusNames=ERGA_CDS_03060;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
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: Heme chaperone required for the biogenesis of c-type
CC cytochromes. Transiently binds heme delivered by CcmC and transfers the
CC heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
CC {ECO:0000255|HAMAP-Rule:MF_01959}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01959}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01959}; Periplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_01959}.
CC -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01959}.
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DR EMBL; CR925677; CAI27758.1; -; Genomic_DNA.
DR RefSeq; WP_011255463.1; NC_006831.1.
DR AlphaFoldDB; Q5FHG0; -.
DR SMR; Q5FHG0; -.
DR PRIDE; Q5FHG0; -.
DR EnsemblBacteria; CAI27758; CAI27758; ERGA_CDS_03060.
DR GeneID; 56785032; -.
DR KEGG; erg:ERGA_CDS_03060; -.
DR HOGENOM; CLU_079503_1_1_5; -.
DR OMA; TFRVGGM; -.
DR OrthoDB; 1724595at2; -.
DR BioCyc; ERUM302409:ERGA_RS01575-MON; -.
DR Proteomes; UP000000533; 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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR GO; GO:0017003; P:protein-heme linkage; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01959; CcmE; 1.
DR InterPro; IPR004329; CcmE.
DR InterPro; IPR036127; CcmE-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR34128; PTHR34128; 1.
DR Pfam; PF03100; CcmE; 1.
DR SUPFAM; SSF82093; SSF82093; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis; Heme;
KW Iron; Membrane; Metal-binding; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..134
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_0000238808"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TOPO_DOM 29..134
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 120
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
SQ SEQUENCE 134 AA; 15250 MW; 1DADB99E8327DC1F CRC64;
MKRKYRRLFV VIITLSIFAG SVVFVLGKLK NNVSFFYTPT ELLSSSLINR PNIRIGGMVV
KGTVQKYDDS IVFHITDLKN YIKVVYKGIL PPLFSEGSWI VAKGKMVNGK FIASEILAKH
DENYMPNKYK TNNL