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MEPA_ECO45
ID   MEPA_ECO45              Reviewed;         274 AA.
AC   B7MG92;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=ECS88_2476;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR03754.1; -; Genomic_DNA.
DR   RefSeq; WP_001043802.1; NC_011742.1.
DR   AlphaFoldDB; B7MG92; -.
DR   SMR; B7MG92; -.
DR   MEROPS; M74.001; -.
DR   EnsemblBacteria; CAR03754; CAR03754; ECS88_2476.
DR   KEGG; ecz:ECS88_2476; -.
DR   HOGENOM; CLU_052496_0_0_6; -.
DR   OMA; VRPWWGH; -.
DR   Proteomes; UP000000747; 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_1000186093"
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
 
 
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