MEPA_ECOK1
ID MEPA_ECOK1 Reviewed; 274 AA.
AC A1ADH7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Penicillin-insensitive murein endopeptidase {ECO:0000255|HAMAP-Rule:MF_01623};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01623};
DE AltName: Full=D-alanyl-D-alanine-endopeptidase {ECO:0000255|HAMAP-Rule:MF_01623};
DE Short=DD-endopeptidase {ECO:0000255|HAMAP-Rule:MF_01623};
DE Flags: Precursor;
GN Name=mepA {ECO:0000255|HAMAP-Rule:MF_01623}; OrderedLocusNames=Ecok1_22230;
GN ORFNames=APECO1_4236;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
CC -!- FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-
CC diamino-pimelyl amide bond that connects peptidoglycan strands. Likely
CC plays a role in the removal of murein from the sacculus.
CC {ECO:0000255|HAMAP-Rule:MF_01623}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01623};
CC Note=Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the
CC active site. Zn(2+) ion 2 is bound at the dimer interface by residues
CC from both subunits. {ECO:0000255|HAMAP-Rule:MF_01623};
CC -!- SUBUNIT: Dimer. {ECO:0000255|HAMAP-Rule:MF_01623}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01623}.
CC -!- SIMILARITY: Belongs to the peptidase M74 family. {ECO:0000255|HAMAP-
CC Rule:MF_01623}.
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DR EMBL; CP000468; ABJ01717.1; -; Genomic_DNA.
DR RefSeq; WP_001043802.1; NC_008563.1.
DR AlphaFoldDB; A1ADH7; -.
DR SMR; A1ADH7; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; ABJ01717; ABJ01717; APECO1_4236.
DR KEGG; ecv:APECO1_4236; -.
DR HOGENOM; CLU_052496_0_0_6; -.
DR OMA; VRPWWGH; -.
DR Proteomes; UP000008216; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1380.10; -; 1.
DR HAMAP; MF_01623; MepA; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR005073; Peptidase_M74.
DR Pfam; PF03411; Peptidase_M74; 1.
DR PIRSF; PIRSF018455; MepA; 1.
DR SUPFAM; SSF55166; SSF55166; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Periplasm;
KW Protease; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT CHAIN 20..274
FT /note="Penicillin-insensitive murein endopeptidase"
FT /id="PRO_0000292554"
FT REGION 227..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT DISULFID 44..265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT DISULFID 187..235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT DISULFID 216..223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
SQ SEQUENCE 274 AA; 30196 MW; 12509E91B4FE2A29 CRC64;
MNKTAIALLA LLASSASLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT LPIQSEHYQV
MRTDQRRYFG HPDLVMFIQR LSRQVSNLGM GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH VVPALWKPEI FSLIKLAAQD KDVTRIFVNP
AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVI
