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Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase (EC 3.4.-.-) (EC 3.4.17.13) (Lipoprotein Spr) (Murein hydrolase MepS)

 MEPS_ECOLI              Reviewed;         188 AA.
P0AFV4; O08016; P77685;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
05-JUL-2017, entry version 85.
RecName: Full=Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase;
EC=3.4.-.-;
EC=3.4.17.13;
AltName: Full=Lipoprotein Spr;
AltName: Full=Murein hydrolase MepS;
Flags: Precursor;
Name=mepS; Synonyms=spr, yeiV; OrderedLocusNames=b2175, JW2163;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9158724; DOI=10.1089/mdr.1996.2.63;
Hara H., Abe N., Nakakouji M., Nishimura Y., Horiuchi K.;
"Overproduction of penicillin-binding protein 7 suppresses
thermosensitive growth defect at low osmolarity due to an spr mutation
of Escherichia coli.";
Microb. Drug Resist. 2:63-72(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
FUNCTION AS A MUREIN DD-ENDOPEPTIDASE, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF CYS-94.
STRAIN=K12;
PubMed=23062283; DOI=10.1111/mmi.12058;
Singh S.K., SaiSree L., Amrutha R.N., Reddy M.;
"Three redundant murein endopeptidases catalyse an essential cleavage
step in peptidoglycan synthesis of Escherichia coli K12.";
Mol. Microbiol. 86:1036-1051(2012).
[6]
STRUCTURE BY NMR OF 63-188, PROBABLE ACTIVE SITE, AND PROBABLE
SUBUNIT.
PubMed=18715016; DOI=10.1021/bi8010779;
Aramini J.M., Rossi P., Huang Y.J., Zhao L., Jiang M., Maglaqui M.,
Xiao R., Locke J., Nair R., Rost B., Acton T.B., Inouye M.,
Montelione G.T.;
"Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from
Escherichia coli: structural evidence for a novel cysteine peptidase
catalytic triad.";
Biochemistry 47:9715-9717(2008).
-!- FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-
meso-diaminopimelic acid (mDAP) cross-links. Its role is probably
to cleave D-Ala-mDAP cross-links to allow insertion of new glycans
and thus cell wall expansion. Functionally redundant with MepM and
MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala
peptide bonds. Partially suppresses a prc disruption mutant.
{ECO:0000269|PubMed:23062283, ECO:0000269|PubMed:9158724}.
-!- CATALYTIC ACTIVITY: GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-
diaminopimelyl-D-alanine + H(2)O = GlcNAc-MurNAc-L-alanyl-gamma-D-
glutamyl-meso-diaminopimelate + D-alanine.
-!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide
biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-
anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
-!- DISRUPTION PHENOTYPE: Unable to grow on nutrient agar at 42
degrees Celsius. A triple mepS-mepH-mepM mutant is inviable,
whereas a double mepS-mepM will grow on a nutrient-poor medium but
not on a rich medium, suggesting the 3 endopeptidases are
functionally redundant in vivo. Depletion experiments of the
double or triple mutants lead to cell lysis, as well as
significantly decreased incorporation of mDAP into peptidogylcan
sacculi and increased amounts of the enzyme's substrate (Tetra-
Tetra-anhydro muropeptide). {ECO:0000269|PubMed:23062283,
ECO:0000269|PubMed:9158724}.
-!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D86610; BAA13140.1; -; Genomic_DNA.
EMBL; U00096; AAC75236.1; -; Genomic_DNA.
EMBL; AP009048; BAA15983.1; -; Genomic_DNA.
PIR; F64986; F64986.
RefSeq; NP_416680.1; NC_000913.3.
RefSeq; WP_000241011.1; NZ_LN832404.1.
PDB; 2K1G; NMR; -; A=63-188.
PDBsum; 2K1G; -.
ProteinModelPortal; P0AFV4; -.
SMR; P0AFV4; -.
BioGrid; 4261093; 195.
IntAct; P0AFV4; 8.
STRING; 316385.ECDH10B_2333; -.
MEROPS; C40.004; -.
PaxDb; P0AFV4; -.
PRIDE; P0AFV4; -.
EnsemblBacteria; AAC75236; AAC75236; b2175.
EnsemblBacteria; BAA15983; BAA15983; BAA15983.
GeneID; 946686; -.
KEGG; ecj:JW2163; -.
KEGG; eco:b2175; -.
PATRIC; fig|511145.12.peg.2263; -.
EchoBASE; EB3829; -.
EcoGene; EG14076; mepS.
eggNOG; ENOG4107TT5; Bacteria.
eggNOG; COG0791; LUCA.
HOGENOM; HOG000229978; -.
InParanoid; P0AFV4; -.
KO; K13694; -.
PhylomeDB; P0AFV4; -.
BioCyc; EcoCyc:G7147-MONOMER; -.
BioCyc; MetaCyc:G7147-MONOMER; -.
UniPathway; UPA00963; -.
EvolutionaryTrace; P0AFV4; -.
PRO; PR:P0AFV4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0004175; F:endopeptidase activity; IDA:EcoCyc.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0000270; P:peptidoglycan metabolic process; IDA:EcoCyc.
GO; GO:0009254; P:peptidoglycan turnover; IMP:CACAO.
InterPro; IPR000064; NLP_P60_dom.
Pfam; PF00877; NLPC_P60; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
Complete proteome; Hydrolase; Lipoprotein; Membrane; Palmitate;
Protease; Reference proteome; Signal; Thiol protease.
SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 27 188 Murein DD-endopeptidase MepS/Murein LD-
carboxypeptidase.
/FTId=PRO_0000019763.
ACT_SITE 94 94 Nucleophile. {ECO:0000305}.
ACT_SITE 145 145 Proton acceptor. {ECO:0000305}.
LIPID 27 27 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
LIPID 27 27 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
MUTAGEN 94 94 C->A: Loss of DD-endopeptidase activity,
no complementation of double mepS-mepM
deletion mutants.
{ECO:0000269|PubMed:23062283}.
HELIX 66 77 {ECO:0000244|PDB:2K1G}.
HELIX 94 104 {ECO:0000244|PDB:2K1G}.
HELIX 114 117 {ECO:0000244|PDB:2K1G}.
HELIX 118 120 {ECO:0000244|PDB:2K1G}.
STRAND 121 124 {ECO:0000244|PDB:2K1G}.
HELIX 126 128 {ECO:0000244|PDB:2K1G}.
STRAND 133 139 {ECO:0000244|PDB:2K1G}.
TURN 140 142 {ECO:0000244|PDB:2K1G}.
STRAND 143 151 {ECO:0000244|PDB:2K1G}.
STRAND 154 159 {ECO:0000244|PDB:2K1G}.
TURN 160 162 {ECO:0000244|PDB:2K1G}.
STRAND 163 168 {ECO:0000244|PDB:2K1G}.
HELIX 172 177 {ECO:0000244|PDB:2K1G}.
STRAND 178 183 {ECO:0000244|PDB:2K1G}.
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


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