PBPA_NEIGO
ID PBPA_NEIGO Reviewed; 798 AA.
AC O05131;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
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 gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RC STRAIN=FA19;
RX PubMed=9098083; DOI=10.1128/jb.179.8.2783-2787.1997;
RA Ropp P.A., Nicholas R.A.;
RT "Cloning and characterization of the ponA gene encoding penicillin-binding
RT protein 1 from Neisseria gonorrhoeae and Neisseria meningitidis.";
RL J. Bacteriol. 179:2783-2787(1997).
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). Essential for cell wall synthesis.
CC {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; U72876; AAB52536.1; -; Genomic_DNA.
DR RefSeq; WP_003687357.1; NZ_WHPL01000002.1.
DR AlphaFoldDB; O05131; -.
DR SMR; O05131; -.
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 1: Evidence at protein level;
KW Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9098083"
FT CHAIN 2..798
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083169"
FT TOPO_DOM 2..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..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..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; 88495 MW; FBA4BA9D5CB0995A CRC64;
MIKKILTTCF GLFFGFCVFG VGLVAIAILV TYPKLPSLDS LQHYQPKMPL TIYSADGEVI
GMYGEQRREF TKIGDFPEVL RNAVIAAEDK RFYRHWGVDV WGVARAAVGN VVSGSVQSGA
STITQQVAKN FYLSSEKTFT RKFNEVLLAY KIEQSLSKDK ILELYFNQIY LGQRAYGFAS
AAQIYFNKNV RDLTLAEAAM LAGLPKAPSA YNPIVNPERA KLRQKYILNN MLEEKMITVQ
QRDQALNEEL HYERFVRKID QSALYVAEMV RRELYEKYGE DAYTQGFKVY TTVRTDHQKA
ATEALRKALR NFDRGSSYRG AENYIDLSKS EDVEETVSQY LSGLYTVDKM VPAVVLDVTK
KKNVVIQLPG GRRVALDRRA LGFAARAVDN EKMGEDRIRR GAVIRVKNNG GRWAVVQEPL
LQGALVSLDA KTGAVRALVG GYDFHSKTFN RAVQAMRQPG STFKPFVYSA ALSKGMTAST
VVNDAPISLP GKGPNGSVWT PKNSDGRYSG YITLRQALTA SKNMVSIRIL MSIGVGYAQQ
YIRRFGFRPS ELPASLSMAL GTGETTPLKV AEAYSVFANG GYRVSSHVID KIYDRDGRLR
AQMQPLVAGQ NAPQAIDPRN AYIMYKIMQD VVRVGTARGA AALGRTDIAG KTGTTNDNKD
AWFVGFNPDV VTAVYIGFDK PKSMGRAGYG GTIAVPVWVD YMRFALKGKQ GKGMKMPEGV
VSSNGEYYMK ERMVTDPGLM LDNSGIAPQP SRRAKEDDEA AVENEQQGRS DETRQDVQET
PVLPSNTDSK QQQLDSLF
