ID CCME_YERPG Reviewed; 164 AA.
AC A9R7X6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 02-NOV-2016, entry version 60.
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=YpAngola_A0391;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/JB.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y.,
RA Mou S., Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola
RT reveals new insights into the evolution and pangenome of the plague
RT bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
CC -!- FUNCTION: Heme chaperone required for the biogenesis of c-type
CC cytochromes. Transiently binds heme delivered by CcmC and
CC transfers the heme to apo-cytochromes in a process facilitated by
CC CcmF and CcmH. {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
CC {ECO:0000255|HAMAP-Rule:MF_01959}.
CC -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01959}.
DR EMBL; CP000901; ABX86786.1; -; Genomic_DNA.
DR RefSeq; WP_002209697.1; NZ_CP009935.1.
DR ProteinModelPortal; A9R7X6; -.
DR EnsemblBacteria; ABX86786; ABX86786; YpAngola_A0391.
DR KEGG; ypg:YpAngola_A0391; -.
DR PATRIC; 18569706; VBIYerPes97331_0675.
DR HOGENOM; HOG000009661; -.
DR KO; K02197; -.
DR OMA; HVEFAVH; -.
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: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-HAMAP.
DR HAMAP; MF_01959; CcmE; 1.
DR InterPro; IPR004329; CcmE.
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;
KW Heme; Iron; Membrane; Metal-binding; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 164 Cytochrome c-type biogenesis protein
FT CcmE.
FT /FTId=PRO_1000189063.
FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255|HAMAP-
FT Rule:MF_01959}.
FT TRANSMEM 9 29 Helical; Signal-anchor for type II
FT membrane protein. {ECO:0000255|HAMAP-
FT Rule:MF_01959}.
FT TOPO_DOM 30 164 Periplasmic. {ECO:0000255|HAMAP-
FT Rule:MF_01959}.
FT METAL 134 134 Iron (heme axial ligand).
FT {ECO:0000255|HAMAP-Rule:MF_01959}.
FT BINDING 130 130 Heme (covalent; via pros nitrogen).
FT {ECO:0000255|HAMAP-Rule:MF_01959}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 4 137 ipfam:CcmE [T]
FT MYHIT 2 147 ihamap:CcmE [T]
SQ SEQUENCE 164 AA; 18033 MW; 5EF4E74F50596559 CRC64;
MNPRRKSRLY LAMVVLIGIS LTTTLVLYAL RSNIDLFYTP GEILQGKGER HEKPAIGQRL
RIGGMVMPGS VQRDAKTLEM SFQVYDARGA VTVTYTGILP DLFREGQGVV AQGVFAEGNT
VHAKEVLAKH DEKYTPPEVE EAMKENHSRP AAAYRGTNTT GNAL
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