ID   PBP7_SHIFL              Reviewed;         310 AA.
AC   P0AFI6; P33364;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
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; OrderedLocusNames=SF2219, S2348;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN43742.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17561.1; -; Genomic_DNA.
DR   RefSeq; NP_708035.3; NC_004337.2.
DR   RefSeq; WP_001319943.1; NZ_WPGW01000017.1.
DR   AlphaFoldDB; P0AFI6; -.
DR   SMR; P0AFI6; -.
DR   STRING; 198214.SF2219; -.
DR   MEROPS; S11.002; -.
DR   EnsemblBacteria; AAN43742; AAN43742; SF2219.
DR   EnsemblBacteria; AAP17561; AAP17561; S2348.
DR   GeneID; 1025374; -.
DR   GeneID; 58388953; -.
DR   KEGG; sfl:SF2219; -.
DR   KEGG; sfx:S2348; -.
DR   PATRIC; fig|198214.7.peg.2657; -.
DR   HOGENOM; CLU_027070_0_3_6; -.
DR   OrthoDB; 1499212at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Hydrolase;
KW   Peptidoglycan synthesis; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..310
FT                   /note="D-alanyl-D-alanine endopeptidase"
FT                   /id="PRO_0000045117"
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