ID   MEPA_CITK8              Reviewed;         274 AA.
AC   A8ADQ0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CKO_00457;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000822; ABV11613.1; -; Genomic_DNA.
DR   RefSeq; WP_012131440.1; NC_009792.1.
DR   AlphaFoldDB; A8ADQ0; -.
DR   SMR; A8ADQ0; -.
DR   STRING; 290338.CKO_00457; -.
DR   MEROPS; M74.001; -.
DR   EnsemblBacteria; ABV11613; ABV11613; CKO_00457.
DR   GeneID; 45134704; -.
DR   KEGG; cko:CKO_00457; -.
DR   HOGENOM; CLU_052496_0_0_6; -.
DR   OMA; VRPWWGH; -.
DR   OrthoDB; 1681877at2; -.
DR   Proteomes; UP000008148; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01623"
FT   CHAIN           20..274
FT                   /note="Penicillin-insensitive murein endopeptidase"
FT                   /id="PRO_1000069595"
FT   REGION          225..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;  30149 MW;  0E8E2DD0787C1C97 CRC64;
     MKKTALALLA LLVSSASLAA TPWQKITHPV PGSAQSIGGF SNGCIVGADT LPVQSEHYQV
     MRTDQRRYFG HPDLVMFIQR LSTQVSNLGF GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
     IFLQLPKTRW TQAQLLRPQA IDLVSRDGKH VVPSLWKPEI SSLIKLAAED NDVTRIFVNP
     AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
     SWFEPPEPGT TKPEKKTPPP LPPSCQALLD EHVL