CCME_KLEP7
ID CCME_KLEP7 Reviewed; 152 AA.
AC A6TA84;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=KPN78578_20440; ORFNames=KPN_02077;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR77505.1; -; Genomic_DNA.
DR RefSeq; WP_004143391.1; NC_009648.1.
DR AlphaFoldDB; A6TA84; -.
DR SMR; A6TA84; -.
DR STRING; 272620.KPN_02077; -.
DR EnsemblBacteria; ABR77505; ABR77505; KPN_02077.
DR GeneID; 56938327; -.
DR GeneID; 64294960; -.
DR KEGG; kpn:KPN_02077; -.
DR HOGENOM; CLU_079503_1_0_6; -.
DR OMA; VTIHFRV; -.
DR Proteomes; UP000000265; 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; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_1000070820"
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..152
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 134
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 152 AA; 16766 MW; BA93CCF1F098D0C6 CRC64;
MQARRKTRLY IVLAVLAGLG LTVSLTLYAL SSNIDLFYTP GEIIYGKTET RALPHTGQRL
RVGGYVQPGS LQRDPQTLDV RFKLYDARGV VDVSYKGILP DLFREGQGVV AQGVLDGERH
ITAQQVLAKH DENYTPPEVK NAMTPEKTGA QP
