Cytochrome c-type biogenesis protein CcmE - Escherichia coli (strain K12)

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P69490 (CCME_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome c-type biogenesis protein CcmE

Alternative name(s):
Cytochrome c maturation protein E
Heme chaperone CcmE

Gene names

Name:	ccmE
Synonyms:	yejS
Ordered Locus Names:	b2197, JW2185

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. HAMAP-Rule MF_01959
Subunit structure	Forms a ternary complex with CcmC and CcmD. Interacts with CcmF. Shuttles between CcmC and CcmF for heme delivery. Ref.6 Ref.7 Ref.9
Subcellular location	Cell inner membrane; Single-pass type II membrane protein; Periplasmic side Potential. Note: Stabilized by CcmD in the membrane. HAMAP-Rule MF_01959
Sequence similarities	Belongs to the CcmE/CycJ family.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytochrome complex assembly Inferred from electronic annotation. Source: UniProtKB-KW protein-heme linkage Inferred from direct assay Ref.4. Source: EcoCyc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to external side of plasma membrane, in periplasmic space Inferred from direct assay Ref.4. Source: EcoCyc
Molecular_function	heme binding Inferred from direct assay Ref.4. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ccmC	P0ABM1	3	EBI-1128007,EBI-2123469

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 159

159

Cytochrome c-type biogenesis protein CcmE HAMAP-Rule MF_01959

PRO_0000201575

Regions

Topological domain

1 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

30 – 159

130

Periplasmic Potential

Sites

Metal binding

134

Iron (heme axial ligand)

Binding site

130

Heme (covalent; via pros nitrogen)

Experimental info

Mutagenesis

130

H → A: Abolishes heme binding. Ref.8

Mutagenesis

130

H → C: Can still form a covalent bond with heme, but blocks heme release transfer to cytochrome c. Ref.8

Secondary structure

159

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P69490 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: FA0585B8CD6446FC
Show »

FASTA

159

17,698

        10         20         30         40         50         60 
MNIRRKNRLW IACAVLAGLA LTIGLVLYAL RSNIDLFYTP GEILYGKRET QQMPEVGQRL 

        70         80         90        100        110        120 
RVGGMVMPGS VQRDPNSLKV TFTIYDAEGS VDVSYEGILP DLFREGQGVV VQGELEKGNH 

       130        140        150 
ILAKEVLAKH DENYTPPEVE KAMEANHRRP ASVYKDPAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Automated multiplex sequencing of the E.coli genome." Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M. Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / BHB2600.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Prototype of a heme chaperone essential for cytochrome c maturation." Schulz H., Hennecke H., Thoeny-Meyer L. Science 281:1197-1200(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 131-140, HEME-BINDING.
[5]	"Escherichia coli genes required for cytochrome c maturation." Thoeny-Meyer L., Fischer F., Kunzler P., Ritz D., Hennecke H. J. Bacteriol. 177:4321-4326(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, GENE NAME.
[6]	"Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation." Ren Q., Thoeny-Meyer L. J. Biol. Chem. 276:32591-32596(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCMC.
[7]	"A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c." Ren Q., Ahuja U., Thoeny-Meyer L. J. Biol. Chem. 277:7657-7663(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCMF.
[8]	"Biochemical and mutational characterization of the heme chaperone CcmE reveals a heme binding site." Enggist E., Schneider M.J., Schulz H., Thoeny-Meyer L. J. Bacteriol. 185:175-183(2003) [PubMed] [Europe PMC] [Abstract] Cited for: HEME-BINDING, MUTAGENESIS OF HIS-130.
[9]	"CcmD is involved in complex formation between CcmC and the heme chaperone CcmE during cytochrome c maturation." Ahuja U., Thoeny-Meyer L. J. Biol. Chem. 280:236-243(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCMD.
[10]	"NMR structure of the heme chaperone CcmE reveals a novel functional motif." Enggist E., Thoeny-Meyer L., Guntert P., Pervushin K. Structure 10:1551-1557(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 30-159.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00008 Genomic DNA. Translation: AAA16389.1.
U00096 Genomic DNA. Translation: AAC75257.1.
AP009048 Genomic DNA. Translation: BAE76660.1.

PIR

C64989.

RefSeq

NP_416701.1. NC_000913.2.
YP_490435.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SR3	NMR	-	A	30-159	[»]

ProteinModelPortal

P69490.

SMR

P69490. Positions 30-143.

ModBase

Search...

Protein-protein interaction databases

IntAct

P69490. 6 interactions.

MINT

MINT-1503318.

STRING

511145.b2197.

Proteomic databases

PRIDE

P69490.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75257; AAC75257; b2197.
BAE76660; BAE76660; BAE76660.

GeneID

12931489.
946697.

KEGG

ecj:Y75_p2158.
eco:b2197.

PATRIC

32119753. VBIEscCol129921_2286.

Organism-specific databases

EchoBASE

EB1986.

EcoGene

EG12055. ccmE.

Phylogenomic databases

eggNOG

COG2332.

HOGENOM

HOG000009661.

K02197.

OMA

FYTPSQI.

ProtClustDB

PRK13165.

Enzyme and pathway databases

BioCyc

EcoCyc:CCME-MONOMER.
ECOL316407:JW2185-MONOMER.

Gene expression databases

Genevestigator

P69490.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

HAMAP

MF_01959. CcmE.

InterPro

IPR004329. CcmE.
IPR012340. NA-bd_OB-fold.
[Graphical view]

Pfam

PF03100. CcmE. 1 hit.
[Graphical view]

SUPFAM

SSF82093. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P69490.

Entry information

Entry name

CCME_ECOLI

Accession

Primary (citable) accession number: P69490
Secondary accession number(s): P33928, Q2MAP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents