MEPA_SHIDS
ID MEPA_SHIDS Reviewed; 274 AA.
AC Q32DK9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=SDY_2527;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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; CP000034; ABB62596.1; -; Genomic_DNA.
DR RefSeq; WP_001043835.1; NC_007606.1.
DR RefSeq; YP_404087.1; NC_007606.1.
DR AlphaFoldDB; Q32DK9; -.
DR SMR; Q32DK9; -.
DR STRING; 300267.SDY_2527; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; ABB62596; ABB62596; SDY_2527.
DR KEGG; sdy:SDY_2527; -.
DR PATRIC; fig|300267.13.peg.3043; -.
DR HOGENOM; CLU_052496_0_0_6; -.
DR OMA; VRPWWGH; -.
DR Proteomes; UP000002716; 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_0000292557"
FT REGION 227..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; 30175 MW; EF91A870104E3301 CRC64;
MNKTAIALLA LLASSVSLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT LPIQSEHYQV
MRTDQRRYFG HPDLVMFIQR LSSQVSNLGM GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH VVSTLWKPEI FSLIKLAAQD KDVTRIFVNP
AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVI
