Penicillin-insensitive murein endopeptidase precursor

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P0C0T5 (MEPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Penicillin-insensitive murein endopeptidase
EC=3.4.24.-

Alternative name(s):
D-alanyl-D-alanine-endopeptidase
Short name=DD-endopeptidase

Gene names

Name:	mepA
Ordered Locus Names:	b2328, JW2325

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the removal of murein from the sacculus. May also facilitate integration of nascent murein strands into the sacculus by cleaving the peptide bonds between neighboring strands in mature murein. Ref.5
Catalytic activity	Splits the D-alanyl-gamma-meso-2,6-diamino-pimelyl peptide bond connecting neighboring peptidoglycan strands. HAMAP-Rule MF_01623
Cofactor	Binds 2 zinc ions per subunit. Zinc ion 1 is bound in the active site. Zinc ion 2 is bound at the dimer interface by residues from both subunits.
Enzyme regulation	Inhibited by Zn²⁺ at 10 mM and by metal chelating agents EDTA and 1,10-phenanthroline. HAMAP-Rule MF_01623
Subunit structure	Dimer.
Subcellular location	Periplasm HAMAP-Rule MF_01623.
Miscellaneous	In E.coli there are three murein endopeptidases: two are penicillin sensitive (DacB and PbpG), the other (MepA) not. HAMAP-Rule MF_01623
Sequence similarities	Belongs to the peptidase M74 family.
Biophysicochemical properties	pH dependence: Optimum pH is 5-8. Ref.5
Mass spectrometry	Molecular mass is 28295 Da from positions 20 - 274. Ref.5

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from direct assay PubMed 1369491. Source: EcoCyc proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from expression pattern PubMed 11344143. Source: EcoCyc
Cellular_component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular_function	endopeptidase activity Inferred from mutant phenotype Ref.1 PubMed 6343788. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: HAMAP serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.1

Chain

20 – 274

255

Penicillin-insensitive murein endopeptidase HAMAP-Rule MF_01623

PRO_0000028520

Sites

Metal binding

110

Zinc 1

Metal binding

113

Zinc 1

Metal binding

120

Zinc 1

Metal binding

147

Zinc 2

Metal binding

150

Zinc 2

Metal binding

211

Zinc 1

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

113

H → A: Strongly reduces enzyme activity. Ref.5

Mutagenesis

120

D → A: Strongly reduces enzyme activity. Ref.5

Mutagenesis

209

H → A: Strongly reduces enzyme activity. Ref.5

Mutagenesis

211

H → A: Strongly reduces enzyme activity. Ref.5

Secondary structure

274

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0C0T5 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: EF91AFD4B381019A
Show »

FASTA

274

30,137

        10         20         30         40         50         60 
MNKTAIALLA LLASSASLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT LPIQSEHYQV 

        70         80         90        100        110        120 
MRTDQRRYFG HPDLVMFIQR LSSQVSNLGM GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD 

       130        140        150        160        170        180 
IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH VVSTLWKPEI FSLIKLAAQD KDVTRIFVNP 

       190        200        210        220        230        240 
AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP SGDGCGAELQ 

       250        260        270 
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of mepA, the structural gene of the penicillin-insensitive murein endopeptidase from Escherichia coli." Keck W., van Leeuwen A.M., Huber M., Goodell E.W. Mol. Microbiol. 4:209-219(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-30. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"Peptidoglycan amidase MepA is a LAS metallopeptidase." Marcyjaniak M., Odintsov S.G., Sabala I., Bochtler M. J. Biol. Chem. 279:43982-43989(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-274 AND IN COMPLEX WITH ZINC ION, INHIBITORS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, MUTAGENESIS OF HIS-113; ASP-120; HIS-209 AND HIS-211.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16909 mRNA. Translation: CAA34782.1.
U00096 Genomic DNA. Translation: AAC75388.1.
AP009048 Genomic DNA. Translation: BAA16184.1.

PIR

S08345.

RefSeq

NP_416831.1. NC_000913.2.
YP_490570.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TZP	X-ray	1.40	A/B	20-274	[»]
1U10	X-ray	2.40	A/B/C/D/E/F	20-274	[»]

ProteinModelPortal

P0C0T5.

SMR

P0C0T5. Positions 20-274.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0C0T5. 1 interaction.

STRING

511145.b2328.

Protein family/group databases

MEROPS

M74.001.

Proteomic databases

PaxDb

P0C0T5.

PRIDE

P0C0T5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75388; AAC75388; b2328.
BAA16184; BAA16184; BAA16184.

GeneID

12930653.
946812.

KEGG

ecj:Y75_p2294.
eco:b2328.

PATRIC

32120029. VBIEscCol129921_2424.

Organism-specific databases

EchoBASE

EB0575.

EcoGene

EG10580. mepA.

Phylogenomic databases

eggNOG

COG3770.

HOGENOM

HOG000276210.

K07261.

OMA

SHQMGLD.

ProtClustDB

PRK09429.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10580-MONOMER.
ECOL316407:JW2325-MONOMER.
MetaCyc:EG10580-MONOMER.

Gene expression databases

Genevestigator

P0C0T5.

Family and domain databases

Gene3D

3.30.1380.10. 1 hit.

HAMAP

MF_01623. MepA.

InterPro

IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR005073. Peptidase_M74.
[Graphical view]

Pfam

PF03411. Peptidase_M74. 1 hit.
[Graphical view]

PIRSF

PIRSF018455. MepA. 1 hit.

SUPFAM

SSF55166. Hedgehog_sig_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0C0T5.

Entry information

Entry name

MEPA_ECOLI

Accession

Primary (citable) accession number: P0C0T5
Secondary accession number(s): P14007

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 68 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

Peptidase families

Classification of peptidase families and list of entries

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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group 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