MEPM_ECOLI
ID MEPM_ECOLI Reviewed; 440 AA.
AC P0AFS9; 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 123.
DE RecName: Full=Murein DD-endopeptidase MepM;
DE EC=3.4.24.-;
DE AltName: Full=Murein hydrolase MepM;
DE AltName: Full=ORFU;
GN Name=mepM; Synonyms=yebA; OrderedLocusNames=b1856, JW5304;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.
RC STRAIN=K12 / EMG2;
RA Robison K., O'Keeffe T., Church G.M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-440.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1732206; DOI=10.1128/jb.174.3.702-710.1992;
RA Karow M.L., Georgopoulos C.;
RT "Isolation and characterization of the Escherichia coli msbB gene, a
RT multicopy suppressor of null mutations in the high-temperature requirement
RT gene htrB.";
RL J. Bacteriol. 174:702-710(1992).
RN [6]
RP POSSIBLE SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / TB28;
RX PubMed=19525345; DOI=10.1128/jb.00505-09;
RA Uehara T., Dinh T., Bernhardt T.G.;
RT "LytM-domain factors are required for daughter cell separation and rapid
RT ampicillin-induced lysis in Escherichia coli.";
RL J. Bacteriol. 191:5094-5107(2009).
RN [7]
RP FUNCTION AS A MUREIN DD-ENDOPEPTIDASE, COFACTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=23062283; DOI=10.1111/mmi.12058;
RA Singh S.K., SaiSree L., Amrutha R.N., Reddy M.;
RT "Three redundant murein endopeptidases catalyse an essential cleavage step
RT in peptidoglycan synthesis of Escherichia coli K12.";
RL Mol. Microbiol. 86:1036-1051(2012).
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. Partially
CC suppresses an mepS disruption mutant. {ECO:0000269|PubMed:23062283}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23062283};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23062283};
CC Note=Zinc, although calcium also allows some activity.
CC {ECO:0000269|PubMed:23062283};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Note=Uniform peripheral location, with
CC partial enrichment at cell poles.
CC -!- DISRUPTION PHENOTYPE: Cells are shorter in a single mutant, while
CC triple envC-nlpD-mepM disruptions have defects in septation and cell
CC separation and form long filaments (15-fold longer) and further yet by
CC the quadruple disruption mutant (envC-nlpD-mepM-ygeR, over 21-fold
CC longer). Quadruple mutants are less sensitive to ampicillin lysis
CC (PubMed:19525345). A triple mepS-mepH-mepM mutant is inviable, whereas
CC a double mepS-mepM will grow on a nutrient-poor medium but not on a
CC rich medium, suggesting the 3 endopeptidases are functionally redundant
CC in vivo. Depletion experiments of the double or triple mutants lead to
CC cell lysis, as well as significantly decreased incorporation of mDAP
CC into peptidogylcan sacculi and increased amounts of the enzyme's
CC substrate (Tetra-Tetra-anhydro muropeptide) (PubMed:23062283).
CC {ECO:0000269|PubMed:19525345, ECO:0000269|PubMed:23062283}.
CC -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74926.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15664.2; -; Genomic_DNA.
DR EMBL; U38702; AAA81029.1; ALT_INIT; Genomic_DNA.
DR EMBL; M77039; AAA24180.1; -; Genomic_DNA.
DR RefSeq; NP_416370.2; NC_000913.3.
DR RefSeq; WP_001184045.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P0AFS9; -.
DR SMR; P0AFS9; -.
DR BioGRID; 4260352; 385.
DR STRING; 511145.b1856; -.
DR MEROPS; M23.011; -.
DR PaxDb; P0AFS9; -.
DR PRIDE; P0AFS9; -.
DR EnsemblBacteria; AAC74926; AAC74926; b1856.
DR EnsemblBacteria; BAA15664; BAA15664; BAA15664.
DR GeneID; 66674254; -.
DR GeneID; 946376; -.
DR KEGG; ecj:JW5304; -.
DR KEGG; eco:b1856; -.
DR PATRIC; fig|1411691.4.peg.392; -.
DR EchoBASE; EB0013; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_026846_0_2_6; -.
DR InParanoid; P0AFS9; -.
DR OMA; GPHVCYR; -.
DR PhylomeDB; P0AFS9; -.
DR BioCyc; EcoCyc:EG10013-MON; -.
DR BioCyc; MetaCyc:EG10013-MON; -.
DR UniPathway; UPA00963; -.
DR PRO; PR:P0AFS9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0004175; F:endopeptidase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
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:0000270; P:peptidoglycan metabolic process; IDA:EcoCyc.
DR GO; GO:0009254; P:peptidoglycan turnover; IMP:CACAO.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..440
FT /note="Murein DD-endopeptidase MepM"
FT /id="PRO_0000026826"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..440
FT /note="Periplasmic"
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"
FT CONFLICT 90
FT /note="A -> P (in Ref. 4; AAA81029)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> T (in Ref. 4; AAA81029)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="T -> S (in Ref. 4; AAA81029)"
FT /evidence="ECO:0000305"
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
