CCME_VIBCM
ID CCME_VIBCM Reviewed; 160 AA.
AC C3LP04;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, 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=VCM66_1977;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP06280.1; -; Genomic_DNA.
DR RefSeq; WP_001069622.1; NC_012578.1.
DR AlphaFoldDB; C3LP04; -.
DR SMR; C3LP04; -.
DR EnsemblBacteria; ACP06280; ACP06280; VCM66_1977.
DR GeneID; 57740680; -.
DR KEGG; vcm:VCM66_1977; -.
DR HOGENOM; CLU_079503_1_0_6; -.
DR OMA; HVEFAVH; -.
DR Proteomes; UP000001217; Chromosome I.
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..160
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_1000189056"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TOPO_DOM 30..160
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 128
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 132
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 160 AA; 17753 MW; C470027AC4E8AC1A CRC64;
MNPRRKKRLG VVLAILFGLS ATIGLIIYAL NQNMDLFYTP TELVYGKEGK KPEIGQRLRI
GGMVVEGSVK RDPNSLKVSF DLHDVGPSIT VTYDGILPDL FREGQGIVAQ GVLVEPTKIE
AFEVLAKHDE NYMPPEIAEA MKKTHAPLQY SQEQKQGSDQ
