MEPM_SHIFL
ID MEPM_SHIFL Reviewed; 440 AA.
AC P0AFT1; 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 109.
DE RecName: Full=Murein DD-endopeptidase MepM;
DE EC=3.4.24.-;
DE AltName: Full=Murein hydrolase MepM;
GN Name=mepM; Synonyms=yebA; OrderedLocusNames=SF1866, S1932;
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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN43423.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17247.1; -; Genomic_DNA.
DR RefSeq; NP_707716.1; NC_004337.2.
DR RefSeq; WP_001184045.1; NZ_UIQL01000048.1.
DR AlphaFoldDB; P0AFT1; -.
DR SMR; P0AFT1; -.
DR STRING; 198214.SF1866; -.
DR MEROPS; M23.011; -.
DR EnsemblBacteria; AAN43423; AAN43423; SF1866.
DR EnsemblBacteria; AAP17247; AAP17247; S1932.
DR GeneID; 1025021; -.
DR GeneID; 66674254; -.
DR KEGG; sfl:SF1866; -.
DR KEGG; sfx:S1932; -.
DR PATRIC; fig|198214.7.peg.2224; -.
DR HOGENOM; CLU_026846_0_2_6; -.
DR OMA; GPHVCYR; -.
DR OrthoDB; 1891666at2; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..440
FT /note="Murein DD-endopeptidase MepM"
FT /id="PRO_0000045125"
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
