ID   MEPM_ECOL6              Reviewed;         440 AA.
AC   P0AFT0; O07981; P24204; P76283;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Murein DD-endopeptidase MepM;
DE            EC=3.4.24.-;
DE   AltName: Full=Murein hydrolase MepM;
GN   Name=mepM; Synonyms=yebA; OrderedLocusNames=c2270;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-meso-
CC       diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave
CC       D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell
CC       wall expansion. Functionally redundant with MepM and MepH (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80727.1; -; Genomic_DNA.
DR   RefSeq; WP_001184045.1; NC_004431.1.
DR   AlphaFoldDB; P0AFT0; -.
DR   SMR; P0AFT0; -.
DR   STRING; 199310.c2270; -.
DR   MEROPS; M23.011; -.
DR   EnsemblBacteria; AAN80727; AAN80727; c2270.
DR   GeneID; 66674254; -.
DR   KEGG; ecc:c2270; -.
DR   eggNOG; COG0739; Bacteria.
DR   HOGENOM; CLU_026846_0_2_6; -.
DR   OMA; GPHVCYR; -.
DR   BioCyc; ECOL199310:C2270-MON; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR045834; Csd3_N2.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR013731; OapA_N.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF19425; Csd3_N2; 1.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF08525; OapA_N; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..440
FT                   /note="Murein DD-endopeptidase MepM"
FT                   /id="PRO_0000045124"
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..141
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   440 AA;  49058 MW;  30431410A5B1A7F7 CRC64;
     MQQIARSVAL AFNNLPRPHR VMLGSLTVLT LAVAVWRPYV YHRDATPIVK TIELEQNEIR
     SLLPEASEPI DQAAQEDEAI PQDELDDKIA GEAGVHEYVV STGDTLSSIL NQYGIDMGDI
     TQLAAADKEL RNLKIGQQLS WTLTADGELQ RLTWEVSRRE TRTYDRTAAN GFKMTSEMQQ
     GEWVNNLLKG TVGGSFVASA RNAGLTSAEV SAVIKAMQWQ MDFRKLKKGD EFAVLMSREM
     LDGKREQSQL LGVRLRSEGK DYYAIRAEDG KFYDRNGTGL AKGFLRFPTA KQFRISSNFN
     PRRTNPVTGR VAPHRGVDFA MPQGTPVLSV GDGEVVVAKR SGAAGYYVAI RHGRSYTTRY
     MHLRKILVKP GQKVKRGDRI ALSGNTGRST GPHLHYEVWI NQQAVNPLTA KLPRTEGLTG
     SDRREFLAQA KEIVPQLRFD