PBPA_NEILA
ID PBPA_NEILA Reviewed; 798 AA.
AC O87579;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRL 3716;
RA Ropp P.A., Nicholas R.A.;
RT "Nucleotide sequence of the ponA gene encoding penicillin-binding protein 1
RT from Neisseria lactamica.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF085689; AAC35363.1; -; Genomic_DNA.
DR AlphaFoldDB; O87579; -.
DR SMR; O87579; -.
DR STRING; 486.B2G52_04360; -.
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; 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; 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_0000083170"
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 378..700
FT /note="Transpeptidase"
FT REGION 739..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..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 461
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 798 AA; 88109 MW; 3B9C7672B86935D6 CRC64;
MIKKIMTTCF GLVFGLCVFA VGLLAIAILA TYPKLPSLDS LQHYQPKMPL TVYSADGKII
GIYGEQRREF TKIGDFPEVL RNAVIAAEDK RFYQHWGVDV WGVARAVVGN IVSGSMQSGA
STITQQVAKN FYLSSEKTFT RKFNEALLAY KIEQSLSKDK ILELYFNQIY LGQRAYGFAS
AAQIYFNKDV RDLTLAEAAM LAGLPKAPSA YNPIVNPERA KLRQKYILNN MLEEKMITLQ
QRDQALNEEL HYERFVQKID QSALYVAEMV RQELYEKYGE DAYTQGLKVY TTVRTDHQKA
ATEALRKALR NFDRGSSYRG AESYIDLGRD EDAEEAVSQY LSGLYTVDKM VPAVVLDVTK
KKNVVIQLPG GKRVTLDRRA LGFAARAVDN EKMGEDRIRR GAVIRVRNNG GRWAVVQEPL
LQGALVSLDA KTGAVRALVG GYDFHSKTFN RATQAMRQPG STFKPFVYSA ALSKGMTAST
MINDAPISLP GKGPNGSVWT PKNSDGRYSG YITLRQALTA SKNMVSIRIL MSIGVGYAQQ
YIRRFGFKPS ELPVSLSMAL GTGETTPLRI AEAYSVFANG GYRVSSYVID KIYDSEGRLR
AQMQPLVAGQ NAPQAIDPRN AYIMYKIMQD VVRVGTARGA SALGRSDIAG KTGTTNDNKD
AWFVGFNPDV VTAVYIGFDK PKSMGRAGYG GTIAVPVWVD YMRFALKGRP GKGMKMPDGV
VAGNGEYYMK EHMVTDPGLM LDNGGAAPQP SRRVKEDDGG AAEGGRQEAD DESRQDMQET
PVLPSNTDSK RQQLDSLF
