MEPA_SALCH
ID MEPA_SALCH Reviewed; 274 AA.
AC Q57LX1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=SCH_2385;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX66291.1; -; Genomic_DNA.
DR RefSeq; WP_001540544.1; NC_006905.1.
DR AlphaFoldDB; Q57LX1; -.
DR SMR; Q57LX1; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; AAX66291; AAX66291; SCH_2385.
DR KEGG; sec:SCH_2385; -.
DR HOGENOM; CLU_052496_0_0_6; -.
DR OMA; VRPWWGH; -.
DR Proteomes; UP000000538; 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_0000044579"
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; 30249 MW; CD58367670A546C4 CRC64;
MKKTAIALLA WFVSSASLAA TPWQKITHPV PGAAQSIASF ANGCIIGADT LPVQSDNYQV
MRTDQRRYFG HPDLVMFIQR LSHQAQQRGL GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
IFLQLPKTRW SQAQLLRPQA LDLVSRDGKH VVPSRWSSDI ASLIKLAAQD NDVTRIFVNP
AIKQQLCLDA GSDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVL
