ID   MEPA_PECAS              Reviewed;         281 AA.
AC   Q6D2M7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Penicillin-insensitive murein endopeptidase;
DE            EC=3.4.24.-;
DE   AltName: Full=D-alanyl-D-alanine-endopeptidase;
DE            Short=DD-endopeptidase;
DE   Flags: Precursor;
GN   Name=mepA; OrderedLocusNames=ECA3068;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit in the active site. {ECO:0000250};
CC   -!- SUBUNIT: Dimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M74 family. {ECO:0000305}.
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DR   EMBL; BX950851; CAG75967.1; -; Genomic_DNA.
DR   RefSeq; WP_011094592.1; NC_004547.2.
DR   AlphaFoldDB; Q6D2M7; -.
DR   SMR; Q6D2M7; -.
DR   STRING; 218491.ECA3068; -.
DR   MEROPS; M74.001; -.
DR   EnsemblBacteria; CAG75967; CAG75967; ECA3068.
DR   GeneID; 57209753; -.
DR   KEGG; eca:ECA3068; -.
DR   PATRIC; fig|218491.5.peg.3101; -.
DR   eggNOG; COG3770; Bacteria.
DR   HOGENOM; CLU_052496_0_0_6; -.
DR   OMA; VRPWWGH; -.
DR   OrthoDB; 1681877at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..281
FT                   /note="Penicillin-insensitive murein endopeptidase"
FT                   /id="PRO_0000044578"
FT   REGION          230..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..270
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..228
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  31013 MW;  0BC5648BD8BC6108 CRC64;
     MKQGLIGVLA LALGATLLSS AVWAKTPWQE IAHPVAGTPQ SIGSFSNGCI IGAQPLPLQS
     LDYQVMRVDQ RRYFGHPDLL AFIHRLSTEV KRTTSGNVLV GDMGMPVGGR FSSGHASHQS
     GLDVDIWLQL PRQRWSEQQL LKPQPIDLVN ASGLNVNPRV WRPEVTTLIK TAALDSDVTR
     IFVNPAIKKQ LCAEAGHDRD WLRKVRPWFA HRAHMHVRLR CPADSLECQE QSEPPIGDGC
     GAELTSWFQP KQPSSEAPEK TTPPPLPPSC QALLDRHFAA R