ID   MEPA_SALPA              Reviewed;         274 AA.
AC   Q5PCX1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SPA0481;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(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;
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; CP000026; AAV76483.1; -; Genomic_DNA.
DR   RefSeq; WP_000750430.1; NC_006511.1.
DR   AlphaFoldDB; Q5PCX1; -.
DR   SMR; Q5PCX1; -.
DR   MEROPS; M74.001; -.
DR   EnsemblBacteria; AAV76483; AAV76483; SPA0481.
DR   KEGG; spt:SPA0481; -.
DR   HOGENOM; CLU_052496_0_0_6; -.
DR   OMA; VRPWWGH; -.
DR   Proteomes; UP000008185; 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_0000044580"
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   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;  30254 MW;  08634E354A288E02 CRC64;
     MKKTAIALLA WFVSSASLAA TPWQKITHPV PGAAQSIGSF ANGCIIGADT LPVQSDNYQV
     MRTDQRRYFG HPDLVMFIQR LSHQAQQRGL GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
     IFLQLPKTRW SQAQLLRPQA LDLVSRDGKH VVPSRWSSDI ASLIKLAAQD NDVTRIFVNP
     AIKQQLCLDA GSDRDWLRKV RPWFQHRAHM RVRLRCPADS LECEDQPLPP PGDGCGAELQ
     SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVL