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 27-MAR-2024, entry version 96. 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; Bacillota; 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}. 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; 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 KEGG; cno:NT01CX_1810; -. DR PATRIC; fig|386415.7.peg.913; -. DR eggNOG; COG0744; Bacteria. DR HOGENOM; CLU_006354_2_2_9; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008220; Chromosome. 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; Biosynthetic peptidoglycan transglycosylase-like; 1. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1. DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1. DR Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR SUPFAM; SSF53955; Lysozyme-like; 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 //