ID   PBPA_STROR              Reviewed;         637 AA.
AC   Q00573;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Penicillin-binding protein 1A;
DE            Short=PBP-1A;
DE   Includes:
DE     RecName: Full=Penicillin-insensitive transglycosylase;
DE              EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE     AltName: Full=Peptidoglycan TGase;
DE   Includes:
DE     RecName: Full=Penicillin-sensitive transpeptidase;
DE              EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE     AltName: Full=DD-transpeptidase;
DE   Flags: Fragment;
GN   Name=ponA;
OS   Streptococcus oralis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1624444; DOI=10.1128/jb.174.13.4517-4523.1992;
RA   Martin C., Briese T., Hakenbeck R.;
RT   "Nucleotide sequences of genes encoding penicillin-binding proteins from
RT   Streptococcus pneumoniae and Streptococcus oralis with high homology to
RT   Escherichia coli penicillin-binding proteins 1a and 1b.";
RL   J. Bacteriol. 174:4517-4523(1992).
CC   -!- FUNCTION: Cell wall formation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000250|UniProtKB:P02918};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000250|UniProtKB:P02918};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000305}.
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DR   EMBL; M90528; AAA26958.1; -; Genomic_DNA.
DR   PIR; B42893; B42893.
DR   AlphaFoldDB; Q00573; -.
DR   SMR; Q00573; -.
DR   STRING; 1303.SORDD17_00136; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   PRIDE; Q00573; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Carboxypeptidase; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase;
KW   Multifunctional enzyme; Peptidoglycan synthesis; Protease; Secreted;
KW   Transferase.
FT   CHAIN           1..>637
FT                   /note="Penicillin-binding protein 1A"
FT                   /id="PRO_0000083181"
FT   REGION          62..224
FT                   /note="Transglycosylase"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   REGION          298..612
FT                   /note="Transpeptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   ACT_SITE        91
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   ACT_SITE        371
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   NON_TER         637
SQ   SEQUENCE   637 AA;  70892 MW;  A6D198BCEA603A63 CRC64;
     MNKQTILRIA KYISICFLTV FIAAIMLGGG LFLYYVSNAP ALSESKLVAT TSSKIYDNND
     ELIADLGSER RVNAQANEIP TDLVNAIVSI EDHRFFNHRG IDTIRILGAT LRNLRGGGGL
     QGASTLTQQL IKLTYFSTST SDQTLSRKAQ EAWLAVQLEQ KATKQEILTY YINKVYMSNG
     NYGMQTAAQS YYGKDLKDLS IPQLALLAGM PQAPNQYDPY SHPEAAQERR NLVLSEMKGQ
     GYITAEQYEK AINTPITDGL QSLKSANSYP PYMDNYLKEV IDQVEQETGY NLLTTGMEVY
     TNVDSKVQQR LWDIYNTDEY VNYPDDELQV ASTIVDVTDG KVIAQLGARH QSSNVSFGIN
     QAVETNRDWG STMKPITDYA PALEYGVYDS TASIVHDSPY NYPGTSTPVY NWDKSYFGNI
     TLQYALQQSR NVPAVETLEK VGLDRAKTFL NGLGIDYPSI HYANAISSNT TESDKKYGAS
     SEKMAAAYAA FANGGIYPKP MYINKIVFSD GSSKEFSDSG TRAMKETTAY MMTDMMKTVL
     AYGTGRGAYL PWLPQAGKTG TSNYTDDEIE NYIKNTGYVA PDEMFVGYTR KYSMAVWTGY
     SNRLTPIVGD GFYVAAKVYR SMMTYLSEDD HPGDWTM