MEPS_ECO57
ID MEPS_ECO57 Reviewed; 188 AA.
AC P0AFV6; O08016; P77685;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase;
DE EC=3.4.-.-;
DE EC=3.4.17.13;
DE AltName: Full=Lipoprotein Spr;
DE AltName: Full=Murein hydrolase MepS;
DE Flags: Precursor;
GN Name=mepS; Synonyms=spr; OrderedLocusNames=Z3434, ECs3067;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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. Also has
CC weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-
CC glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-
CC glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl;
CC Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13;
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; AE005174; AAG57313.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36490.1; -; Genomic_DNA.
DR PIR; C91012; C91012.
DR PIR; E85856; E85856.
DR RefSeq; NP_311094.1; NC_002695.1.
DR RefSeq; WP_000241011.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFV6; -.
DR BMRB; P0AFV6; -.
DR SMR; P0AFV6; -.
DR STRING; 155864.EDL933_3342; -.
DR MEROPS; C40.004; -.
DR EnsemblBacteria; AAG57313; AAG57313; Z3434.
DR EnsemblBacteria; BAB36490; BAB36490; ECs_3067.
DR GeneID; 67414541; -.
DR GeneID; 916771; -.
DR KEGG; ece:Z3434; -.
DR KEGG; ecs:ECs_3067; -.
DR PATRIC; fig|386585.9.peg.3199; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_9_1_6; -.
DR OMA; MHAVNDK; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Hydrolase; Lipoprotein; Membrane; Palmitate; Protease;
KW Reference proteome; Signal; Thiol protease.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 27..188
FT /note="Murein DD-endopeptidase MepS/Murein LD-
FT carboxypeptidase"
FT /id="PRO_0000045241"
FT DOMAIN 64..185
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 188 AA; 21040 MW; 65DCEEDBDDC76098 CRC64;
MVKSQPILRY ILRGIPAIAV AVLLSACSAN NTAKNMHPET RAVGSETSSL QASQDEFENL
VRNVDVKSRI MDQYADWKGV RYRLGGSTKK GIDCSGFVQR TFREQFGLEL PRSTYEQQEM
GKSVSRSNLR TGDLVLFRAG STGRHVGIYI GNNQFVHAST SSGVIISSMN EPYWKKRYNE
ARRVLSRS
