PBPA_CLOTE
ID PBPA_CLOTE Reviewed; 790 AA.
AC Q891X1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=CTC_02242;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36724.1; -; Genomic_DNA.
DR RefSeq; WP_011100385.1; NC_004557.1.
DR AlphaFoldDB; Q891X1; -.
DR SMR; Q891X1; -.
DR STRING; 212717.CTC_02242; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; Q891X1; -.
DR EnsemblBacteria; AAO36724; AAO36724; CTC_02242.
DR GeneID; 64179681; -.
DR KEGG; ctc:CTC_02242; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; QQNTGGD; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001412; 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..790
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000321879"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..790
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 61..230
FT /note="Transglycosylase"
FT /evidence="ECO:0000250"
FT REGION 363..656
FT /note="Transpeptidase"
FT /evidence="ECO:0000250"
FT REGION 720..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 402
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 790 AA; 88212 MW; 685396E0B8742B73 CRC64;
MANVRKRRKK KNEHKALRLT FITLLMVFLF SCVAAAGVGL AMIKAAPPLD VDKVLNPSEP
SVIYDDKNKL VDTVISDTYR TIVSYEDVPD NLKNAFISIE DERFFNHRGI DYKRVFGAFF
RNISNKLKGK SALQGASTIT QQLVRNTLLS QEVRIKRKVQ EMYLSIQLEK KVSKEQILEA
YMNTIPLGGS AYGIEAASKQ YFGKSVKDLN LIESAFIAGL PQSPSTFYNA AMSQKNTERY
INRTKLVLGK MREHNYISKE DFDKSMAYID KNKIPLKTSN INISRLNYEW FSREIIKQVK
KDLMNEYKIS PTEADKTIMY GGLKIYGTMD KSLQDFSQNT LDNLDGILGI NSKDYSGIIQ
PEASVSIVDY KTGNVKVLIG GRGKQPPLSF NRATEFYRAP GSTIKPLTVY GPAIDTKTST
AASSYNDAPV PEEIGKLYDK EPYNPKNSPN IYEGKMTLRE ALMKSKNVIS VRIEHELGLK
TGAEYGKKFG LTIDDSMDGT SMAALSLGQL SAKTGVSGTN TLGMAAAYGV FGNKGALSKP
VVYKKVVDRT GKVLLENKYA SSKVMSPEAA YILYDLLKGP VSYTPGATGM KANFGPMARG
KTGTSNQSSD LWFAGLSPYY SAAVWIGKDD YSPFTNEFGR YIGSSDAALI WKLIMGEAHK
NLEYKTIEKP AGVTEAYVCS KSGKIPSSSC PRDSIKLEYF IEGTIPGEIC DYHTGIFNNN
KDKDDDDDDK DKDKEDEEEN KDEKNEDKKE AKDNTKNKDK DKKKDNDRKI DMDKKPDSSK
RKRKMIKPQI
