PBPA_CLOPS
ID PBPA_CLOPS Reviewed; 820 AA.
AC Q0SRL7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=CPR_1930;
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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}.
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; CP000312; ABG87192.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SRL7; -.
DR SMR; Q0SRL7; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; ABG87192; ABG87192; CPR_1930.
DR KEGG; cpr:CPR_1930; -.
DR OMA; QQNTGGD; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001824; 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..820
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000321878"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..820
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 72..244
FT /note="Transglycosylase"
FT /evidence="ECO:0000250"
FT REGION 378..663
FT /note="Transpeptidase"
FT /evidence="ECO:0000250"
FT REGION 732..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 417
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 820 AA; 90968 MW; 025D8E5E6F9A92C0 CRC64;
MTERKREYKD RKQKKNSPKN QSKVTKFLKW FFIGVLLLGI TAITIVGFYV LSIIRSSPEL
DVQAIQSLNQ PSILYDDQGN FMDNVITREQ RYVVKSDEIP DNLKKAFVAI EDERFYEHKG
IDIKRIAGVI ASNIKGKLSG SNTVQGASTI TQQLIKNAVL TNEVSYERKI KEMYLALELE
KHLSKDEILT TYLNTIPMGG YQYGVSAAAQ RFFSKNVSDL NLIECAYLGG LTQAPTSYDG
LSEINKENPS RYLNRTKSVL FKMHELGYIS SEQYNNAINE IDTNGIKFKP NNKLSKTNFE
WFTRPTITQV KQDLMNKYKY TQDEVDKLIA NGGLKIYTSM DRNLQNNVQK VLDDPNNYKA
ITNNPNEKNE DDVYKLQASA TIIDYKTGHV KALVGGRGEQ PAMSHNRAYY DLKSIGSATK
PLTVYGPAID LGLGGAGSVV NDSPLTNKEL SSTGYKDQPK NEYNSYRGPL TFREAIKISS
NLAAIKVANE VGVSNSIAYG EKLGLVYGPH SRGISTTALG QFQNDPNNPD GGNTYTLASA
FGVFGNNGVK TNAKLYTKVL DSHGNVLLDT STPEEIKIFS PQTSYIVYDM LKDQVESGSA
KPAKFGNIPV AGKTGTTTGD KDYLFAGLTP YYSAAIWIGY DKPREMRTSS GIVTSPIFGK
IMGLAHKGLQ YKEVEQPSGI SKIAVCMDSG LKPTSLCTQD PRGSRVYYDW FINGSAPNQY
CNYHTNSHVN NFNKNNNTTG VNEKNKKQET KTEEIKPNEN NKSNEQTPNT NPDNAPNNVP
NNDNNNSNNI GGNMIPPQNQ TENNTNNGVI TPNQSINNKN
