CCME_ECOLI
ID CCME_ECOLI Reviewed; 159 AA.
AC P69490; P33928; Q2MAP6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=yejS;
GN OrderedLocusNames=b2197, JW2185;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 131-140, AND HEME-BINDING.
RX PubMed=9712585; DOI=10.1126/science.281.5380.1197;
RA Schulz H., Hennecke H., Thoeny-Meyer L.;
RT "Prototype of a heme chaperone essential for cytochrome c maturation.";
RL Science 281:1197-1200(1998).
RN [5]
RP CHARACTERIZATION, AND GENE NAME.
RX PubMed=7635817; DOI=10.1128/jb.177.15.4321-4326.1995;
RA Thoeny-Meyer L., Fischer F., Kunzler P., Ritz D., Hennecke H.;
RT "Escherichia coli genes required for cytochrome c maturation.";
RL J. Bacteriol. 177:4321-4326(1995).
RN [6]
RP INTERACTION WITH CCMC.
RX PubMed=11384983; DOI=10.1074/jbc.m103058200;
RA Ren Q., Thoeny-Meyer L.;
RT "Physical interaction of CcmC with heme and the heme chaperone CcmE during
RT cytochrome c maturation.";
RL J. Biol. Chem. 276:32591-32596(2001).
RN [7]
RP INTERACTION WITH CCMF.
RX PubMed=11744735; DOI=10.1074/jbc.m110979200;
RA Ren Q., Ahuja U., Thoeny-Meyer L.;
RT "A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme
RT chaperone CcmE and CcmH but not with apocytochrome c.";
RL J. Biol. Chem. 277:7657-7663(2002).
RN [8]
RP HEME-BINDING, AND MUTAGENESIS OF HIS-130.
RX PubMed=12486054; DOI=10.1128/jb.185.1.175-183.2003;
RA Enggist E., Schneider M.J., Schulz H., Thoeny-Meyer L.;
RT "Biochemical and mutational characterization of the heme chaperone CcmE
RT reveals a heme binding site.";
RL J. Bacteriol. 185:175-183(2003).
RN [9]
RP INTERACTION WITH CCMD.
RX PubMed=15513913; DOI=10.1074/jbc.m410912200;
RA Ahuja U., Thoeny-Meyer L.;
RT "CcmD is involved in complex formation between CcmC and the heme chaperone
RT CcmE during cytochrome c maturation.";
RL J. Biol. Chem. 280:236-243(2005).
RN [10]
RP STRUCTURE BY NMR OF 30-159.
RX PubMed=12429096; DOI=10.1016/s0969-2126(02)00885-7;
RA Enggist E., Thoeny-Meyer L., Guntert P., Pervushin K.;
RT "NMR structure of the heme chaperone CcmE reveals a novel functional
RT motif.";
RL Structure 10:1551-1557(2002).
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 -!- SUBUNIT: Forms a ternary complex with CcmC and CcmD. Interacts with
CC CcmF. Shuttles between CcmC and CcmF for heme delivery.
CC {ECO:0000269|PubMed:11384983, ECO:0000269|PubMed:11744735,
CC ECO:0000269|PubMed:15513913}.
CC -!- INTERACTION:
CC P69490; P0ABM1: ccmC; NbExp=7; IntAct=EBI-1128007, EBI-2123469;
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}. Note=Stabilized by CcmD in the membrane.
CC -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01959}.
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DR EMBL; U00008; AAA16389.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75257.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76660.1; -; Genomic_DNA.
DR PIR; C64989; C64989.
DR RefSeq; NP_416701.1; NC_000913.3.
DR RefSeq; WP_001026418.1; NZ_STEB01000002.1.
DR PDB; 1SR3; NMR; -; A=30-159.
DR PDBsum; 1SR3; -.
DR AlphaFoldDB; P69490; -.
DR SMR; P69490; -.
DR BioGRID; 4260483; 134.
DR ComplexPortal; CPX-3568; CcmABCDE system I cytochrome c biogenesis complex.
DR DIP; DIP-9255N; -.
DR IntAct; P69490; 8.
DR MINT; P69490; -.
DR STRING; 511145.b2197; -.
DR jPOST; P69490; -.
DR PaxDb; P69490; -.
DR PRIDE; P69490; -.
DR EnsemblBacteria; AAC75257; AAC75257; b2197.
DR EnsemblBacteria; BAE76660; BAE76660; BAE76660.
DR GeneID; 66673908; -.
DR GeneID; 946697; -.
DR KEGG; ecj:JW2185; -.
DR KEGG; eco:b2197; -.
DR PATRIC; fig|1411691.4.peg.39; -.
DR EchoBASE; EB1986; -.
DR eggNOG; COG2332; Bacteria.
DR HOGENOM; CLU_079503_1_0_6; -.
DR InParanoid; P69490; -.
DR OMA; HVEFAVH; -.
DR PhylomeDB; P69490; -.
DR BioCyc; EcoCyc:CCME-MON; -.
DR BioCyc; MetaCyc:CCME-MON; -.
DR EvolutionaryTrace; P69490; -.
DR PRO; PR:P69490; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IC:ComplexPortal.
DR GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1903607; P:cytochrome c biosynthetic process; IDA:EcoCyc.
DR GO; GO:0017004; P:cytochrome complex assembly; IC:ComplexPortal.
DR GO; GO:1904334; P:heme import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0017003; P:protein-heme linkage; IEA:UniProtKB-UniRule.
DR DisProt; DP01729; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Direct protein sequencing; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..159
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_0000201575"
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..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT REGION 132..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
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 MUTAGEN 130
FT /note="H->A: Abolishes heme binding."
FT /evidence="ECO:0000269|PubMed:12486054"
FT MUTAGEN 130
FT /note="H->C: Can still form a covalent bond with heme, but
FT blocks heme release transfer to cytochrome c."
FT /evidence="ECO:0000269|PubMed:12486054"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1SR3"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:1SR3"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1SR3"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:1SR3"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1SR3"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:1SR3"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1SR3"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1SR3"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1SR3"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1SR3"
SQ SEQUENCE 159 AA; 17698 MW; FA0585B8CD6446FC CRC64;
MNIRRKNRLW IACAVLAGLA LTIGLVLYAL RSNIDLFYTP GEILYGKRET QQMPEVGQRL
RVGGMVMPGS VQRDPNSLKV TFTIYDAEGS VDVSYEGILP DLFREGQGVV VQGELEKGNH
ILAKEVLAKH DENYTPPEVE KAMEANHRRP ASVYKDPAS
