PBPA_CLOAB
ID PBPA_CLOAB Reviewed; 809 AA.
AC Q97GR5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CA_C2301;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80257.1; -; Genomic_DNA.
DR PIR; F97183; F97183.
DR RefSeq; NP_348917.1; NC_003030.1.
DR RefSeq; WP_010965598.1; NC_003030.1.
DR AlphaFoldDB; Q97GR5; -.
DR SMR; Q97GR5; -.
DR STRING; 272562.CA_C2301; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR MEROPS; X52.001; -.
DR PRIDE; Q97GR5; -.
DR EnsemblBacteria; AAK80257; AAK80257; CA_C2301.
DR KEGG; cac:CA_C2301; -.
DR PATRIC; fig|272562.8.peg.2498; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OMA; AVQMPYI; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000814; 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..809
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000321872"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..809
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 74..251
FT /note="Transglycosylase"
FT /evidence="ECO:0000250"
FT REGION 381..664
FT /note="Transpeptidase"
FT /evidence="ECO:0000250"
FT REGION 694..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 422
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 809 AA; 88725 MW; 60C5C426D283205C CRC64;
MSDNTKTNSR NKSVKRTKKV KKKKKFGFFK KLFTILFCLF ILLSVAASGV IFAIVKTSPN
LDINGTILNL DQPSQLYDDN NNPMDTVVTN QRRYVVSIKD MPKNLSNAFV SIEDERFYKH
SGIDTKRILG AFYNDIKSKI HKQNSIQGAS TITQQLIKNR MFLNDSLENR ISFKRKIQEA
YLSIKLEQSL SKSQILEAYM NTIFLGVQAN GVEAASRQYF NKSAKDLNLI ECAFIAGLAQ
SPSAYYPFSQ NVAKNPNIYL DRTKLVLYKM RQNNYIDFST YQNAINDLNN NKLAFSQQKI
SNKYTYEWFS IPVVNQVKQD LKSQYHYTDE EIDSLLRDGG LKIYTTMNTS MESNVQNILD
NNSTLKSYSY ADKNGIIQPE AAATLFDYHT GEIKAIVGGR GQQPPSSYNR ADSSNYLRSV
GSSIKPLTVY APAIDTKLAT EDTIVNDSPL SSDVAEKYGS NGVPYNPHND DGGYSGPVNL
KTALTKSINL VAIKLEDKLG LSTGAAYAQK FGLTLNNDDK SSIAALSLGE IRGSNTTTMA
AAYGVFGNNG LYSEPRLYRK VVDKTGKVLL ENNYSTRKVI SPQSAYIMYD LLKGPVSAGG
TGSYARFGDM PVAGKTGTAS DSKNLWFCGL TPYYSAAVWV GNDQPTKLSL GSNDVAEIWG
EIMKMANVNL TVKDIDAPGG VTKIGDSYYI DGTSPSNLSG DDSSSSTASK PQTPTTNTQN
NTNNNVANPN SNNTTNSNTS NSTETPAQNT QQPTPTPTPS TNNTPGNTNT NTNTNNNTNT
NTNTNNNNTN NSSSGNNNPP NNNTTNTNK
