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Protein

Penicillin-insensitive murein endopeptidase

Gene

mepA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Splits the D-alanyl-gamma-meso-2,6-diamino-pimelyl peptide bond connecting neighboring peptidoglycan strands.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. Zn2+ ion 1 is bound in the active site. Zn2+ ion 2 is bound at the dimer interface by residues from both subunits.1 Publication

Enzyme regulationi

Inhibited by Zn2+ at 10 mM and by metal chelating agents EDTA and 1,10-phenanthroline.1 Publication

pH dependencei

Optimum pH is 5-8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101Zinc 11 Publication
Metal bindingi113 – 1131Zinc 11 Publication
Metal bindingi120 – 1201Zinc 11 Publication
Metal bindingi147 – 1471Zinc 21 Publication
Metal bindingi150 – 1501Zinc 21 Publication
Metal bindingi211 – 2111Zinc 11 Publication

GO - Molecular functioni

  • endopeptidase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: UniProtKB-HAMAP
  • peptidase activity Source: EcoCyc
  • serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  • peptidoglycan biosynthetic process Source: EcoCyc
  • peptidoglycan metabolic process Source: EcoCyc
  • response to drug Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiM74.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-insensitive murein endopeptidase (EC:3.4.24.-1 Publication)
Alternative name(s):
D-alanyl-D-alanine-endopeptidase
Short name:
DD-endopeptidase
Gene namesi
Name:mepA
Ordered Locus Names:b2328, JW2325
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10580. mepA.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1131H → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi120 – 1201D → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi209 – 2091H → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi211 – 2111H → A: Strongly reduces enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 274255Penicillin-insensitive murein endopeptidasePRO_0000028520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 2651 Publication
Disulfide bondi187 ↔ 2351 Publication
Disulfide bondi216 ↔ 2231 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0C0T5.
PRIDEiP0C0T5.

Interactioni

Subunit structurei

Dimer.1 Publication

Protein-protein interaction databases

BioGridi4259647. 309 interactions.
IntActiP0C0T5. 1 interaction.
STRINGi511145.b2328.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 254Combined sources
Beta strandi35 – 395Combined sources
Beta strandi42 – 476Combined sources
Beta strandi56 – 616Combined sources
Helixi63 – 653Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 8716Combined sources
Beta strandi93 – 953Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi118 – 1236Combined sources
Helixi132 – 1365Combined sources
Beta strandi148 – 1514Combined sources
Turni153 – 1553Combined sources
Helixi158 – 16912Combined sources
Beta strandi173 – 1786Combined sources
Helixi180 – 18910Combined sources
Helixi195 – 1995Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi207 – 2148Combined sources
Helixi237 – 2415Combined sources
Helixi263 – 2708Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZPX-ray1.40A/B20-274[»]
1U10X-ray2.40A/B/C/D/E/F20-274[»]
ProteinModelPortaliP0C0T5.
SMRiP0C0T5. Positions 20-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0T5.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M74 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105HPZ. Bacteria.
COG3770. LUCA.
HOGENOMiHOG000276210.
InParanoidiP0C0T5.
KOiK07261.
OMAiVRPWWGH.
OrthoDBiEOG6F295X.

Family and domain databases

Gene3Di3.30.1380.10. 1 hit.
HAMAPiMF_01623. MepA.
InterProiIPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR005073. Peptidase_M74.
[Graphical view]
PfamiPF03411. Peptidase_M74. 1 hit.
[Graphical view]
PIRSFiPIRSF018455. MepA. 1 hit.
SUPFAMiSSF55166. SSF55166. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0T5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKTAIALLA LLASSASLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT
60 70 80 90 100
LPIQSEHYQV MRTDQRRYFG HPDLVMFIQR LSSQVSNLGM GTVLIGDMGM
110 120 130 140 150
PAGGRFNGGH ASHQTGLDVD IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH
160 170 180 190 200
VVSTLWKPEI FSLIKLAAQD KDVTRIFVNP AIKQQLCLDA GTDRDWLRKV
210 220 230 240 250
RPWFQHRAHM HVRLRCPADS LECEDQPLPP SGDGCGAELQ SWFEPPKPGT
260 270
TKPEKKTPPP LPPSCQALLD EHVI
Length:274
Mass (Da):30,137
Last modified:December 6, 2005 - v1
Checksum:iEF91AFD4B381019A
GO

Mass spectrometryi

Molecular mass is 28295 Da from positions 20 - 274. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16909 mRNA. Translation: CAA34782.1.
U00096 Genomic DNA. Translation: AAC75388.1.
AP009048 Genomic DNA. Translation: BAA16184.1.
PIRiS08345.
RefSeqiNP_416831.1. NC_000913.3.
WP_001043825.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75388; AAC75388; b2328.
BAA16184; BAA16184; BAA16184.
GeneIDi946812.
KEGGiecj:JW2325.
eco:b2328.
PATRICi32120029. VBIEscCol129921_2424.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16909 mRNA. Translation: CAA34782.1.
U00096 Genomic DNA. Translation: AAC75388.1.
AP009048 Genomic DNA. Translation: BAA16184.1.
PIRiS08345.
RefSeqiNP_416831.1. NC_000913.3.
WP_001043825.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZPX-ray1.40A/B20-274[»]
1U10X-ray2.40A/B/C/D/E/F20-274[»]
ProteinModelPortaliP0C0T5.
SMRiP0C0T5. Positions 20-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259647. 309 interactions.
IntActiP0C0T5. 1 interaction.
STRINGi511145.b2328.

Protein family/group databases

MEROPSiM74.001.

Proteomic databases

PaxDbiP0C0T5.
PRIDEiP0C0T5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75388; AAC75388; b2328.
BAA16184; BAA16184; BAA16184.
GeneIDi946812.
KEGGiecj:JW2325.
eco:b2328.
PATRICi32120029. VBIEscCol129921_2424.

Organism-specific databases

EchoBASEiEB0575.
EcoGeneiEG10580. mepA.

Phylogenomic databases

eggNOGiENOG4105HPZ. Bacteria.
COG3770. LUCA.
HOGENOMiHOG000276210.
InParanoidiP0C0T5.
KOiK07261.
OMAiVRPWWGH.
OrthoDBiEOG6F295X.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0C0T5.
PROiP0C0T5.

Family and domain databases

Gene3Di3.30.1380.10. 1 hit.
HAMAPiMF_01623. MepA.
InterProiIPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR005073. Peptidase_M74.
[Graphical view]
PfamiPF03411. Peptidase_M74. 1 hit.
[Graphical view]
PIRSFiPIRSF018455. MepA. 1 hit.
SUPFAMiSSF55166. SSF55166. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-274 AND IN COMPLEX WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-113; ASP-120; HIS-209 AND HIS-211, ENZYME REGULATION, COFACTOR.

Entry informationi

Entry nameiMEPA_ECOLI
AccessioniPrimary (citable) accession number: P0C0T5
Secondary accession number(s): P14007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In E.coli there are three murein endopeptidases: two are penicillin sensitive (DacB and PbpG), the other (MepA) not.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.