MEPA_YERPA
ID MEPA_YERPA Reviewed; 275 AA.
AC Q1C665;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
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=YPA_2091;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG14057.1; -; Genomic_DNA.
DR RefSeq; WP_002225365.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C665; -.
DR SMR; Q1C665; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; ABG14057; ABG14057; YPA_2091.
DR GeneID; 66844948; -.
DR KEGG; ypa:YPA_2091; -.
DR Proteomes; UP000001971; 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..275
FT /note="Penicillin-insensitive murein endopeptidase"
FT /id="PRO_0000292559"
FT REGION 227..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Pro residues"
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 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..264
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 275 AA; 30293 MW; F9526CF3807D0C02 CRC64;
MKNWIVGMVA LVTMVPVMAA TPWQKITHPV AGSPQSIGGF ANGCVIGAQP LPLESADYQV
MRSDQRRYFG HPDLLNFIHR LSAQAHQQQL GTVLIGDMAM PAGGRFSSGH ASHQSGLDVD
IWLQLPKQRW SQQQLLKPQP IDLVAVDGKR VIPALWQPQI ESLIKLAAKD NDVTRIFVNP
AIKKQLCLDA GADRQWLHKV RPWFAHRAHM HVRLRCPANS LECVDQDTPP PGDGCGAELE
SWFQPPPPSA KPGKTLPPPL PPSCQALLDN HFATE
