MEPA_SHIFL
ID MEPA_SHIFL Reviewed; 274 AA.
AC P0C0T6; P14007;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Penicillin-insensitive murein endopeptidase;
DE EC=3.4.24.-;
DE AltName: Full=D-alanyl-D-alanine-endopeptidase;
DE Short=DD-endopeptidase;
DE Flags: Precursor;
GN Name=mepA; OrderedLocusNames=SF2404, S2539;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M74 family. {ECO:0000305}.
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DR EMBL; AE005674; AAN43917.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17735.1; -; Genomic_DNA.
DR RefSeq; NP_708210.1; NC_004337.2.
DR RefSeq; WP_001043825.1; NZ_WPGW01000016.1.
DR AlphaFoldDB; P0C0T6; -.
DR SMR; P0C0T6; -.
DR STRING; 198214.SF2404; -.
DR MEROPS; M74.001; -.
DR EnsemblBacteria; AAN43917; AAN43917; SF2404.
DR EnsemblBacteria; AAP17735; AAP17735; S2539.
DR GeneID; 1025542; -.
DR GeneID; 58388052; -.
DR KEGG; sfl:SF2404; -.
DR KEGG; sfx:S2539; -.
DR PATRIC; fig|198214.7.peg.2871; -.
DR HOGENOM; CLU_052496_0_0_6; -.
DR OMA; VRPWWGH; -.
DR OrthoDB; 1681877at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0000250"
FT CHAIN 20..274
FT /note="Penicillin-insensitive murein endopeptidase"
FT /id="PRO_0000043377"
FT REGION 228..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:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 44..265
FT /evidence="ECO:0000250"
FT DISULFID 187..235
FT /evidence="ECO:0000250"
FT DISULFID 216..223
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 30137 MW; EF91AFD4B381019A CRC64;
MNKTAIALLA LLASSASLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT LPIQSEHYQV
MRTDQRRYFG HPDLVMFIQR LSSQVSNLGM GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH VVSTLWKPEI FSLIKLAAQD KDVTRIFVNP
AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP SGDGCGAELQ
SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVI
