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Penicillin-binding protein 1A (PBP1) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPA_CLOPE              Reviewed;         679 AA.
Q8XJ01;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
05-JUL-2017, entry version 96.
RecName: Full=Penicillin-binding protein 1A;
Short=PBP1;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
AltName: Full=DD-transpeptidase;
Name=pbpA; OrderedLocusNames=CPE1962;
Clostridium perfringens (strain 13 / Type A).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=195102;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=13 / Type A;
PubMed=11792842; DOI=10.1073/pnas.022493799;
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
"Complete genome sequence of Clostridium perfringens, an anaerobic
flesh-eater.";
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000250|UniProtKB:P02918}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000250|UniProtKB:P02918}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type II membrane protein {ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BA000016; BAB81668.1; -; Genomic_DNA.
ProteinModelPortal; Q8XJ01; -.
DrugBank; DB01060; Amoxicillin.
DrugBank; DB01061; Azlocillin.
DrugBank; DB01602; Bacampicillin.
DrugBank; DB00833; Cefaclor.
DrugBank; DB00456; Cefalotin.
DrugBank; DB01139; Cefapirin.
DrugBank; DB01066; Cefditoren.
DrugBank; DB00267; Cefmenoxime.
DrugBank; DB00229; Cefotiam.
DrugBank; DB01112; Cefuroxime.
DrugBank; DB01147; Cloxacillin.
DrugBank; DB01000; Cyclacillin.
DrugBank; DB04133; Degraded Cephaloridine.
DrugBank; DB00301; Flucloxacillin.
DrugBank; DB00447; Loracarbef.
DrugBank; DB00948; Mezlocillin.
DrugBank; DB00713; Oxacillin.
DrugBank; DB00417; Phenoxymethylpenicillin.
DrugBank; DB01604; Pivampicillin.
DrugBank; DB01605; Pivmecillinam.
CAZy; GT51; Glycosyltransferase Family 51.
EnsemblBacteria; BAB81668; BAB81668; BAB81668.
KEGG; cpe:CPE1962; -.
HOGENOM; HOG000041137; -.
KO; K05366; -.
OMA; WVGFNDS; -.
OrthoDB; POG091H01NC; -.
UniPathway; UPA00219; -.
Proteomes; UP000000818; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 2.
3: Inferred from homology;
Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 679 Penicillin-binding protein 1A.
/FTId=PRO_0000321877.
TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.
TRANSMEM 31 51 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 52 679 Extracellular. {ECO:0000255}.
REGION 72 244 Transglycosylase. {ECO:0000250}.
REGION 378 663 Transpeptidase. {ECO:0000250}.
ACT_SITE 111 111 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 417 417 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
SEQUENCE 679 AA; 75177 MW; FCEE7683E6C07A3B CRC64;
MTERKREHKD RKQNKNSPKN QSKVTKFLKW FFIGILLLGI TAVTVVGIYV LSIIRSSPEL
DVQAIQSLNQ PSILYDDQGN FMDNVITREQ RYVVKSEEIP DNLKKAFVAI EDERFYEHKG
IDIKRIFGVI ASNIKGKLSG SNTVQGASTI TQQLIKNAVL TNEVSYERKI KEMYLALELE
KHLSKDEILT TYLNTIPMGG YQYGVSAAAQ RFFSKNVSDL NLVECAYLGG LTQAPTSYDG
LSEANKENPS RYLNRTKSVL FKMHELGYIS SEQYNDAINE IDTNGIKFTP NNKLSKTNFE
WFTRPAITQV KQDLMDKYKY TQEEVDKLIA NGGLKIYTSM DRNLQNNVQK VLDDPNNYKA
ITNNPNEKNE DGVYKLQASA TIIDYKTGHV KALVGGRGEQ PAMSHNRAYY DLKSIGSATK
PLTVYGPAID LGLGGAGSVV NDSPLSNKEL SSTGYKDQPK NEYNSYRGPL TFREAIKISS
NLAAIKVANE VGVSNSIAYG EKLGLVYGPH SRGISTTALG QFQNDPNNPD GGNTYTLASA
FGVFGNNGVK TNAKLYTKVL DSHGNVILDT STPEETKIFS PQASYIVYDM LKDQVESGSA
KSAKFGNIPV AGKTGTTTGD KDYLFAGLTP YYSAAIWIGY DKPREMRTSS GTVTSPIFGK
IMGLAHKDLQ YKEVDNLVE


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