PBP7_ECOLI
ID PBP7_ECOLI Reviewed; 310 AA.
AC P0AFI5; P33364; Q2MAU5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=D-alanyl-D-alanine endopeptidase;
DE Short=DD-endopeptidase;
DE EC=3.4.21.-;
DE AltName: Full=Penicillin-binding protein 7;
DE Short=PBP-7;
DE Flags: Precursor;
GN Name=pbpG; Synonyms=yohB; OrderedLocusNames=b2134, JW5355;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 198-310.
RX PubMed=6386470; DOI=10.1111/j.1432-1033.1984.tb08473.x;
RA Campbell H.D., Rogers B.L., Young I.G.;
RT "Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of
RT Escherichia coli.";
RL Eur. J. Biochem. 144:367-373(1984).
RN [5]
RP PROTEIN SEQUENCE OF 26-33, AND CHARACTERIZATION.
RX PubMed=7721700; DOI=10.1128/jb.177.8.2074-2079.1995;
RA Henderson T.A., Templin M., Young K.D.;
RT "Identification and cloning of the gene encoding penicillin-binding protein
RT 7 of Escherichia coli.";
RL J. Bacteriol. 177:2074-2079(1995).
RN [6]
RP CHARACTERIZATION.
RX PubMed=7925376; DOI=10.1111/j.1432-1033.1994.00597.x;
RA Romeis T., Holtje J.V.;
RT "Penicillin-binding protein 7/8 of Escherichia coli is a DD-
RT endopeptidase.";
RL Eur. J. Biochem. 224:597-604(1994).
CC -!- FUNCTION: Cell wall formation. May play a specialized role in
CC remodeling the cell wall. Specifically hydrolyzes the DD-
CC diaminopimelate-alanine bonds in high-molecular-mass murein sacculi.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Pbp8 is a proteolytic product of Pbp7.
CC -!- MISCELLANEOUS: In E.coli there are three murein endopeptidases: two are
CC penicillin sensitive (DacB and PbpG), the other (MepA) not.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00007; AAA60496.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75195.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76611.1; -; Genomic_DNA.
DR EMBL; X01067; CAA25532.1; -; Genomic_DNA.
DR PIR; E64981; E64981.
DR RefSeq; NP_416638.4; NC_000913.3.
DR RefSeq; WP_001319943.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0AFI5; -.
DR SMR; P0AFI5; -.
DR BioGRID; 4260453; 247.
DR BioGRID; 851004; 8.
DR DIP; DIP-48108N; -.
DR IntAct; P0AFI5; 9.
DR STRING; 511145.b2134; -.
DR DrugBank; DB01331; Cefoxitin.
DR MEROPS; S11.002; -.
DR jPOST; P0AFI5; -.
DR PaxDb; P0AFI5; -.
DR PRIDE; P0AFI5; -.
DR EnsemblBacteria; AAC75195; AAC75195; b2134.
DR EnsemblBacteria; BAE76611; BAE76611; BAE76611.
DR GeneID; 58388953; -.
DR GeneID; 946662; -.
DR KEGG; ecj:JW5355; -.
DR KEGG; eco:b2134; -.
DR PATRIC; fig|1411691.4.peg.109; -.
DR EchoBASE; EB1952; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_0_3_6; -.
DR InParanoid; P0AFI5; -.
DR OMA; WDIKLTK; -.
DR PhylomeDB; P0AFI5; -.
DR BioCyc; EcoCyc:EG12015-MON; -.
DR BioCyc; MetaCyc:EG12015-MON; -.
DR PRO; PR:P0AFI5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IDA:EcoCyc.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IDA:EcoCyc.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:EcoCyc.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Peptidoglycan synthesis; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:7721700"
FT CHAIN 26..310
FT /note="D-alanyl-D-alanine endopeptidase"
FT /id="PRO_0000027237"
FT ACT_SITE 67
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 33887 MW; 4CD97290757526EE CRC64;
MPKFRVSLFS LALMLAVPFA PQAVAKTAAA TTASQPEIAS GSAMIVDLNT NKVIYSNHPD
LVRPIASISK LMTAMVVLDA RLPLDEKLKV DISQTPEMKG VYSRVRLNSE ISRKDMLLLA
LMSSENRAAA SLAHHYPGGY KAFIKAMNAK AKSLGMNNTR FVEPTGLSVH NVSTARDLTK
LLIASKQYPL IGQLSTTRED MATFSNPTYT LPFRNTNHLV YRDNWNIQLT KTGFTNAAGH
CLVMRTVINN KPVALVVMDA FGKYTHFADA SRLRTWIETG KVMPVPAAAL SYKKQKAAQM
AAAGQTAQND
