MEPS_ECOL6
ID MEPS_ECOL6 Reviewed; 188 AA.
AC P0AFV5; O08016; P77685;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=c2712;
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. 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; AE014075; AAN81166.1; -; Genomic_DNA.
DR RefSeq; WP_000241011.1; NC_004431.1.
DR AlphaFoldDB; P0AFV5; -.
DR BMRB; P0AFV5; -.
DR SMR; P0AFV5; -.
DR STRING; 199310.c2712; -.
DR EnsemblBacteria; AAN81166; AAN81166; c2712.
DR GeneID; 67414541; -.
DR KEGG; ecc:c2712; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_9_1_6; -.
DR OMA; MHAVNDK; -.
DR BioCyc; ECOL199310:C2712-MON; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001410; 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 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_0000045242"
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
