PBPA_CLONN
ID PBPA_CLONN Reviewed; 863 AA.
AC A0PZT1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=NT01CX_1810;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(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}.
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DR EMBL; CP000382; ABK60403.1; -; Genomic_DNA.
DR RefSeq; WP_011721888.1; NC_008593.1.
DR AlphaFoldDB; A0PZT1; -.
DR SMR; A0PZT1; -.
DR STRING; 386415.NT01CX_1810; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; A0PZT1; -.
DR EnsemblBacteria; ABK60403; ABK60403; NT01CX_1810.
DR KEGG; cno:NT01CX_1810; -.
DR PATRIC; fig|386415.7.peg.913; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; AVQMPYI; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008220; 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;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..863
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000321875"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..863
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 71..248
FT /note="Transglycosylase"
FT /evidence="ECO:0000250"
FT REGION 392..674
FT /note="Transpeptidase"
FT /evidence="ECO:0000250"
FT REGION 774..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..863
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 431
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 863 AA; 95824 MW; A0250C35592BC539 CRC64;
MTENRDNKTS QSEKTTQKKK KKKFKAFKII LITFITLIVI SLVTAIGITL AIIKTSPDIN
INEIIAASDA SKIYDDKGEL VDSIITSKKK ILVKYDEVPE NLINAFVSIE DERFFKHSGI
DVKRIAGAFL IDMKNIVSGK PALQGASTIT QQLIKNTVFE THGNSLNDKL RRKVQEWYLA
PKLEKEVGKK SIMEAYLNTI YLGGRAIGVG AAADQYFNVS IDKLDLVQCA FIAGLPQSPS
VYYPYSRTSK KDPSKYINRT KTVLAKMKEN GYISQNEYIS ALAELDTSKS TVTNDESIQT
LGQYTIHKPT NIDEKYNFEW FTRPAIERVK KDLKDIYNYS DDEIEKLLVN GNLKIYTTMN
KDLQVSTQEI IDNDEKLNSL SSSKNNLVEP QASAVLTDYH TGEVKVIIGG RGTQPALAYN
RATNAKVAAG SSIKPLTVYS AAIDSKLATA ATVLEDSPLP EAMSKKYSAP GTNWQPKNAN
GVYSGYLGLR DALKNSVNVY AVKLEDKIGL NTGVKYGEKF GLTFDNVDKN SMAAIALGEL
NRGTNTFTMA NAYGVFGNNG MYSNPRLYTK VLDRNGNVLL ETKTQATQVI SPEAAYIMYD
LLKGPVKEGT ATRIQHTYHS DIPIAGKTGS STKFKNLWFC GLTPYYSGAV WIENKYGQSI
YSSDAAALFG KIMNRAVENL PEKEIEMPEG IIKAEVDRVS GLLPTDLSYK DPRGSQVYTE
LFIKGTVPTE QDNIHVSTKV NKYNGRVSGS YTPSFLTESK VFIKRQSDSE VPLDDDMYVL
PDKDKKSSNK SKHNHNNDAK HDNTNNSEDA TNEASTEPSP NTDTVPEDST NNLDPTKNTE
KKPSDKKNKK HVIKPIIRPK KHF
