MEPA_SALAR
ID MEPA_SALAR Reviewed; 274 AA.
AC A9MJ43;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, 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=SARI_00517;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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}.
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DR EMBL; CP000880; ABX20443.1; -; Genomic_DNA.
DR RefSeq; WP_000750432.1; NC_010067.1.
DR AlphaFoldDB; A9MJ43; -.
DR SMR; A9MJ43; -.
DR STRING; 41514.SARI_00517; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; ABX20443; ABX20443; SARI_00517.
DR KEGG; ses:SARI_00517; -.
DR HOGENOM; CLU_052496_0_0_6; -.
DR OMA; VRPWWGH; -.
DR OrthoDB; 1681877at2; -.
DR Proteomes; UP000002084; 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_1000088093"
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; 30231 MW; 795D47751E2F1336 CRC64;
MKKTAIALLA WFVSSASLAA TPWQKITHPV PGAAQSVGSF ANGCIIGADT LPVQSDNYQV
MRTDQRRYFG HPDLVMFIQR LSHQAHQRGL GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
IFLQLPKTRW SQAQLLRPQA LDLVSRDGKH VVPSRWSSDI ASLIKLAAED NDVTRIFVNP
AIKQQLCLDA GSDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVL
