MEPH_ECOLI
ID MEPH_ECOLI Reviewed; 271 AA.
AC P76190; P78164;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Murein DD-endopeptidase MepH;
DE EC=3.4.-.-;
DE AltName: Full=Murein hydrolase MepH;
DE Flags: Precursor;
GN Name=mepH; Synonyms=ydhO; OrderedLocusNames=b1655, JW5270;
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=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 FUNCTION AS A MUREIN DD-ENDOPEPTIDASE, 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 -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- DISRUPTION PHENOTYPE: A triple mepS-mepH-mepM mutant is inviable,
CC whereas a double mepS-mepM will grow on a nutrient-poor medium but not
CC on a rich medium, suggesting the 3 endopeptidases are functionally
CC redundant in vivo. Depletion experiments of the double or triple
CC mutants lead to cell lysis, as well as significantly decreased
CC incorporation of mDAP into peptidogylcan sacculi and increased amounts
CC of the enzyme's substrate (Tetra-Tetra-anhydro muropeptide).
CC {ECO:0000269|PubMed:23062283}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; U00096; AAC74727.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15421.2; -; Genomic_DNA.
DR PIR; A64923; A64923.
DR RefSeq; NP_416172.1; NC_000913.3.
DR RefSeq; WP_000101193.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P76190; -.
DR SMR; P76190; -.
DR BioGRID; 4259398; 202.
DR STRING; 511145.b1655; -.
DR MEROPS; C40.013; -.
DR PaxDb; P76190; -.
DR PRIDE; P76190; -.
DR EnsemblBacteria; AAC74727; AAC74727; b1655.
DR EnsemblBacteria; BAA15421; BAA15421; BAA15421.
DR GeneID; 945210; -.
DR KEGG; ecj:JW5270; -.
DR KEGG; eco:b1655; -.
DR PATRIC; fig|511145.12.peg.1727; -.
DR EchoBASE; EB3707; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_2_0_6; -.
DR InParanoid; P76190; -.
DR OMA; ILYWGSA; -.
DR PhylomeDB; P76190; -.
DR BioCyc; EcoCyc:G6892-MON; -.
DR BioCyc; MetaCyc:G6892-MON; -.
DR UniPathway; UPA00963; -.
DR PRO; PR:P76190; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase 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: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.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..271
FT /note="Murein DD-endopeptidase MepH"
FT /id="PRO_0000019768"
FT DOMAIN 138..265
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 27..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ SEQUENCE 271 AA; 29917 MW; 4B432592D23B31EF CRC64;
MARINRISIT LCALLFTTLP LTPMAHASKQ ARESSATTHI TKKADKKKST ATTKKTQKTA
KKAASKSTTK SKTASSVKKS SITASKNAKT RSKHAVNKTA SASFTEKCTK RKGYKSHCVK
VKNAASGTLA DAHKAKVQKA TKVAMNKLMQ QIGKPYRWGG SSPRTGFDCS GLVYYAYKDL
VKIRIPRTAN EMYHLRDAAP IERSELKNGD LVFFRTQGRG TADHVGVYVG NGKFIQSPRT
GQEIQITSLS EDYWQRHYVG ARRVMTPKTL R
