PBPA_CLOBL
ID PBPA_CLOBL Reviewed; 827 AA.
AC A7GHV1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Penicillin-binding protein 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=pbpA; OrderedLocusNames=CLI_3142;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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 membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
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; CP000728; ABS42508.1; -; Genomic_DNA.
DR RefSeq; WP_012100804.1; NC_009699.1.
DR AlphaFoldDB; A7GHV1; -.
DR SMR; A7GHV1; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; ABS42508; ABS42508; CLI_3142.
DR KEGG; cbf:CLI_3142; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; AVQMPYI; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002410; Chromosome.
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; -; 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 membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..827
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000321874"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..827
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 57..229
FT /note="Transglycosylase"
FT /evidence="ECO:0000250"
FT REGION 357..641
FT /note="Transpeptidase"
FT /evidence="ECO:0000250"
FT REGION 755..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 398
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 827 AA; 92415 MW; 6890261BA9400825 CRC64;
MGKKKKKRKS SAFKIILNVF LSIFLVAGVA FGGIVFAMIK TAPPLNVQQV LTFDEPSILY
DDKGQYMDKV ITNEQRIVVD YKNVPQNLKN AFVSIEDERF YKHHGVDIKR FTGVILINVT
NKIKRSSKLQ GASTLTQQLI KNTVLSSEVS IKRKVQEMYL SIQLEKELSK DEILGAYMNS
IFLGGNALGV EAASKQYFNK SVKDLSLIEC AFIAGVPQSP SVYYPYSSAS KKNPSIYLNR
TKTVLYKMLD NGYITQNDYN KALKDLDSKK LAFAKPSAPS NKLAYEWFSI PAIEQVKKDL
KTQYKYDDKQ IHNLLVNGGL KIYTTMNKNL QDKTQNTIND AYYLNSYKSN GIIYPQASAV
IMDYHNGEVK TIVGGRGDQP ARSYNRAASY NYLRPAGSSI KPLTVYSAAI DSKKATAATG
FEDSPIPNNI GRKYSSGAPY NPRNTPDIYY GYVNVREALM RSINVVAVKL VDKIGLNTSI
QYAEKFGIPI DQHDRSSIAS LSLGELHKGT NPLIMAQAYG VFGNNGTYTE AKLYTKVVDR
TGKVLLEPKT NTKKVLSPEA AFITYDMLQG PVSESGTGPQ ANFGNMEVRG KTGTSSDMKN
LWFCGLTPYY SAAVWIGNDN SSTVDGVYSS TAARLWGDIM KEFHVNLPYK QVQKPASVVT
ANVDRISGKL PTQLSYRDPR GSTVYNEFFI NGTIPTEYDD IHVEAQINKL TGKLASKFTP
SFLVESRVFL RRDYSPGVEL LDQQWLLPYS IDEGGSLPPT EEKNNSNTRD KNKDKNKDKD
KNKNKDKNPS QDKPNNNNNN NNNDNNNNTK PPENDSNQNH EDNKNKQ
