ID   PBPA_NEIFL              Reviewed;         798 AA.
AC   O87626;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Penicillin-binding protein 1A;
DE            Short=PBP-1a;
DE            Short=PBP1a;
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;
GN   Name=mrcA; Synonyms=ponA;
OS   Neisseria flavescens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13120 / DSM 17633 / CCUG 345 / CIP 73.15 / LMG 5297 / NCTC 8263
RC   / NRL 30009 / N155;
RA   Ropp P.A., Nicholas R.A.;
RT   "Nucleotide sequence of the ponA gene encoding penicillin-binding protein 1
RT   of Neisseria flavescens.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC       from the lipid intermediates. The enzyme has a penicillin-insensitive
CC       transglycosylase N-terminal domain (formation of linear glycan strands)
CC       and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC       linking of the peptide subunits). {ECO:0000250}.
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: Cell inner membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}.
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; AF087677; AAC35856.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87626; -.
DR   SMR; O87626; -.
DR   STRING; 596320.NEIFL0001_1961; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.710.10; -; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR031376; PCB_OB.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF17092; PCB_OB; 1.
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 inner membrane;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW   Peptidoglycan synthesis; Protease; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..798
FT                   /note="Penicillin-binding protein 1A"
FT                   /id="PRO_0000083167"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..798
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          50..218
FT                   /note="Transglycosylase"
FT   REGION          413..699
FT                   /note="Transpeptidase"
FT   REGION          734..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
FT   ACT_SITE        460
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P02919"
SQ   SEQUENCE   798 AA;  87704 MW;  0DDCDF6FD25953AA CRC64;
     MIKKIITTCM GLNNGLALFG VGLIAIAILV TYPKLPSLDS LQHYKPKLPL TIYSSDGQVI
     GVYGEQRREF TKIDDFPKIL KDAVIAAEDK RFYDHWGVDV WGVARAVIGN VMAGGVQSGA
     STITQQVAKN FYLSSERSFT RKFNEALLAY KIEQSLSKDK ILELYFNQIY LGQRAYGFAS
     AAQTYFNKNV NDLTLAEAAM LAGLPKAPSA YNPIVNPERA KLRQAYILNN MLEEGMITLQ
     QRDQALKEEL HYERFVQNID QSALYVAEMA RQELFEKYGE DAYTQGFKVY TTVDTAHQRV
     ATEALRKVLR NFDRGSSYRG AENYIDLSKS DNVEETVSQY LSTLYTVDKM IPAVVLEASR
     KGVQIQLPSG RKVTLNNHAL GFAARAVNNE KMGDDRIRRG SVIRVKGSGD TFTVVQEPLL
     QGALVSLDAK TGAVRALVGG YDYHSKTFNR ATQAMRQPGS TFKPFIYSAA LAKGMTASTM
     INDAPISLPG KGANGKAWNP KNSDGRYAGY ITLRQALTAS KNMVSIRILM SIGIGYAQQY
     IQRFGFKPSE IPASLSMALG AGETTPLRIA EGYSVFANGG YKVSAHVIDK IYDSQGRLRA
     QMQPLVAGEN APQAIDPRNA YIMYKIMQDV VRVGTARGAA TLGRSDIAGK TGTTNDNKDA
     WFVGFNPNVV TAVYIGFDKP RSMGRAGYGG TIAVPVWVEY IGFALKGTSV KPMKAPEGVV
     TNGGEVYMRE RMTTSSDLAL DNSGIRPRPT QPARRAVPNE NRRRAESNTA PAREESDETP
     VLPSNTGNNN RQQLDSLF