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

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Reviewed, UniProtKB/Swiss-Prot P69490 (CCME_ECOLI)

Last modified November 3, 2009. Version 46. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 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.
Sequence similarities	Belongs to the ccmE/cycJ family.

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Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal-anchor Transmembrane
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cytochrome complex assembly Inferred from electronic annotation. Source: UniProtKB-KW protein-heme linkage Inferred from electronic annotation. Source: HAMAP
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.7 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ccmC	P0ABM1	1	EBI-1128007,EBI-2123469
ccmF	P33927	1	EBI-1128007,EBI-763370

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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 MF_01959

PRO_0000201575

Regions

Topological domain

1 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Signal-anchor for type II membrane protein Potential

Topological domain

30 – 159

130

Periplasmic Potential

Sites

Metal binding

134

Iron (heme axial ligand) HAMAP MF_01959

Binding site

130

Heme (covalent; via pros nitrogen) HAMAP MF_01959

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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P69490-1 [UniParc].

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

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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: 9278503] [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: 16738553] [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: 9712585] [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: 7635817] [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: 11384983] [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: 11744735] [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: 12486054] [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: 15513913] [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: 12429096] [Abstract] Cited for: STRUCTURE BY NMR OF 30-159.

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Cross-references

Sequence databases

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

PIR

C64989.

RefSeq

AP_002793.1.
NP_416701.1.

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P69490. 5 interactions.

STRING

P69490.

Genome annotation databases

GeneID

946697.

GenomeReviews

Gene locus JW2185 in contig AP009048_GR.
Gene locus b2197 in contig U00096_GR.

KEGG

ecj:JW2185.
eco:b2197.

Organism-specific databases

EchoBASE

EB1986.

EcoGene

EG12055. ccmE.

CMR

Search...

Phylogenomic databases

HOGENOM

P69490.

OMA

VEKGSLQ.

Enzyme and pathway databases

BioCyc

EcoCyc:CCME-MON.

Gene expression databases

Genevestigator

P69490.

Family and domain databases

HAMAP

MF_01959.
[Tree]

InterPro

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

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

Pfam

PF03100. CcmE. 1 hit.
[Graphical view]

ProDom

PD006742. CcmE. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

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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:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents