ID   PBP7_HAEIN              Reviewed;         292 AA.
AC   P44664;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=D-alanyl-D-alanine endopeptidase;
DE            Short=DD-endopeptidase;
DE            EC=3.4.21.-;
DE   AltName: Full=Penicillin-binding protein 7 homolog;
DE            Short=PBP-7;
DE   Flags: Precursor;
GN   Name=pbpG; OrderedLocusNames=HI_0364;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22022.1; -; Genomic_DNA.
DR   PIR; H64149; H64149.
DR   RefSeq; NP_438525.1; NC_000907.1.
DR   RefSeq; WP_005693802.1; NC_000907.1.
DR   AlphaFoldDB; P44664; -.
DR   SMR; P44664; -.
DR   STRING; 71421.HI_0364; -.
DR   MEROPS; S11.002; -.
DR   EnsemblBacteria; AAC22022; AAC22022; HI_0364.
DR   KEGG; hin:HI_0364; -.
DR   PATRIC; fig|71421.8.peg.381; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_4_1_6; -.
DR   OMA; LVVVQMY; -.
DR   PhylomeDB; P44664; -.
DR   BioCyc; HINF71421:G1GJ1-377-MON; -.
DR   Proteomes; UP000000579; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..292
FT                   /note="D-alanyl-D-alanine endopeptidase"
FT                   /id="PRO_0000027238"
FT   ACT_SITE        45
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  32620 MW;  919633D863314FF7 CRC64;
     MFKKALFILS LCPSFALAQS YVVYDFTHNR VLESHASDSI QPIASVTKLM TANVFLENNK
     NPNCRIAITK EDTDRIKGTG TKLPKNIPIS CNELLKAMLV HSDNYAAHAL SRAAGISRRQ
     FIKKMNEKAH QLGMYSTRFH DSSGLSSYNI SSPMDLVKLA KYSLNKSDIK RLSNLSATYI
     QAGKQKLYIK NTNKLVRDEI FDAAVNKTGY IQESGYNLVF INKHRCKNAT IGVISLNNTS
     SAYRSSFTKS KLEKFGCTAL NGRTIRDVAG EAQYEDGYDE VGFNTLIQKL SK