MEPS_ECOLI
ID MEPS_ECOLI Reviewed; 188 AA.
AC P0AFV4; O08016; P77685;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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, yeiV; OrderedLocusNames=b2175, JW2163;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9158724; DOI=10.1089/mdr.1996.2.63;
RA Hara H., Abe N., Nakakouji M., Nishimura Y., Horiuchi K.;
RT "Overproduction of penicillin-binding protein 7 suppresses thermosensitive
RT growth defect at low osmolarity due to an spr mutation of Escherichia
RT coli.";
RL Microb. Drug Resist. 2:63-72(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION AS A MUREIN DD-ENDOPEPTIDASE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-94.
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).
RN [6]
RP STRUCTURE BY NMR OF 63-188, PROBABLE ACTIVE SITE, AND PROBABLE SUBUNIT.
RX PubMed=18715016; DOI=10.1021/bi8010779;
RA Aramini J.M., Rossi P., Huang Y.J., Zhao L., Jiang M., Maglaqui M.,
RA Xiao R., Locke J., Nair R., Rost B., Acton T.B., Inouye M.,
RA Montelione G.T.;
RT "Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from
RT Escherichia coli: structural evidence for a novel cysteine peptidase
RT catalytic triad.";
RL Biochemistry 47:9715-9717(2008).
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.
CC Partially suppresses a prc disruption mutant.
CC {ECO:0000269|PubMed:23062283, ECO:0000269|PubMed:9158724}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow on nutrient agar at 42 degrees
CC Celsius. A triple mepS-mepH-mepM mutant is inviable, whereas a double
CC mepS-mepM will grow on a nutrient-poor medium but not on a rich medium,
CC suggesting the 3 endopeptidases are functionally redundant in vivo.
CC Depletion experiments of the double or triple mutants lead to cell
CC lysis, as well as significantly decreased incorporation of mDAP into
CC peptidogylcan sacculi and increased amounts of the enzyme's substrate
CC (Tetra-Tetra-anhydro muropeptide). {ECO:0000269|PubMed:23062283,
CC ECO:0000269|PubMed:9158724}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, 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; D86610; BAA13140.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75236.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15983.1; -; Genomic_DNA.
DR PIR; F64986; F64986.
DR RefSeq; NP_416680.1; NC_000913.3.
DR RefSeq; WP_000241011.1; NZ_STEB01000002.1.
DR PDB; 2K1G; NMR; -; A=63-188.
DR PDBsum; 2K1G; -.
DR AlphaFoldDB; P0AFV4; -.
DR BMRB; P0AFV4; -.
DR SMR; P0AFV4; -.
DR BioGRID; 4261093; 195.
DR IntAct; P0AFV4; 8.
DR STRING; 511145.b2175; -.
DR MEROPS; C40.004; -.
DR PaxDb; P0AFV4; -.
DR PRIDE; P0AFV4; -.
DR EnsemblBacteria; AAC75236; AAC75236; b2175.
DR EnsemblBacteria; BAA15983; BAA15983; BAA15983.
DR GeneID; 67414541; -.
DR GeneID; 946686; -.
DR KEGG; ecj:JW2163; -.
DR KEGG; eco:b2175; -.
DR PATRIC; fig|511145.12.peg.2263; -.
DR EchoBASE; EB3829; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_9_1_6; -.
DR InParanoid; P0AFV4; -.
DR OMA; MHAVNDK; -.
DR PhylomeDB; P0AFV4; -.
DR BioCyc; EcoCyc:G7147-MON; -.
DR BioCyc; MetaCyc:G7147-MON; -.
DR UniPathway; UPA00963; -.
DR EvolutionaryTrace; P0AFV4; -.
DR PRO; PR:P0AFV4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0004175; F:endopeptidase activity; IDA:EcoCyc.
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: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 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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Protease; Reference proteome;
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_0000019763"
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"
FT MUTAGEN 94
FT /note="C->A: Loss of DD-endopeptidase activity, no
FT complementation of double mepS-mepM deletion mutants."
FT /evidence="ECO:0000269|PubMed:23062283"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:2K1G"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2K1G"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2K1G"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2K1G"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2K1G"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2K1G"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2K1G"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:2K1G"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2K1G"
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
