PBPA_PSEAE
ID PBPA_PSEAE Reviewed; 822 AA.
AC Q07806;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-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=mrcA; Synonyms=ponA; OrderedLocusNames=PA5045;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Handfield J., Gagnon L., Dargis M., Huletsky A.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7901733; DOI=10.1111/j.1365-2958.1993.tb01744.x;
RA Martin P.R., Hobbs M., Free P.D., Jeske Y., Mattick J.S.;
RT "Characterization of pilQ, a new gene required for the biogenesis of type 4
RT fimbriae in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 9:857-868(1993).
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 inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
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; U73780; AAB39710.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08430.1; -; Genomic_DNA.
DR EMBL; L13867; AAC36826.1; -; Unassigned_DNA.
DR PIR; F83016; F83016.
DR RefSeq; NP_253732.1; NC_002516.2.
DR RefSeq; WP_003114576.1; NZ_QZGE01000002.1.
DR PDB; 4OON; X-ray; 3.20 A; A=36-822.
DR PDBsum; 4OON; -.
DR AlphaFoldDB; Q07806; -.
DR SMR; Q07806; -.
DR STRING; 287.DR97_2400; -.
DR BindingDB; Q07806; -.
DR ChEMBL; CHEMBL3259512; -.
DR DrugBank; DB14879; Cefiderocol.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB00430; Cefpiramide.
DR DrugCentral; Q07806; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; Q07806; -.
DR PRIDE; Q07806; -.
DR DNASU; 881163; -.
DR EnsemblBacteria; AAG08430; AAG08430; PA5045.
DR GeneID; 881163; -.
DR KEGG; pae:PA5045; -.
DR PATRIC; fig|208964.12.peg.5289; -.
DR PseudoCAP; PA5045; -.
DR HOGENOM; CLU_006354_2_4_6; -.
DR InParanoid; Q07806; -.
DR OMA; LAQMAMI; -.
DR PhylomeDB; Q07806; -.
DR BioCyc; PAER208964:G1FZ6-5161-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:Q07806; -.
DR Proteomes; UP000002438; 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; IDA:PseudoCAP.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 3.
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; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 2.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..822
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083173"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..822
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 48..216
FT /note="Transglycosylase"
FT REGION 403..744
FT /note="Transpeptidase"
FT REGION 614..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 461
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 293..312
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 513..518
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 522..532
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 566..577
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 588..592
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 662..677
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 682..687
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 715..721
FT /evidence="ECO:0007829|PDB:4OON"
FT HELIX 734..749
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:4OON"
FT TURN 771..773
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:4OON"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:4OON"
SQ SEQUENCE 822 AA; 91200 MW; 0B1A3F6FA5D492AA CRC64;
MRLLKFLWWT CVTLICGVLL SFSGAYLYLS PSLPSVEALR NVQLQIPLKV YSEDGKLISE
FGEMRRTPIR FADIPQDFIH ALLSAEDDNF ANHYGVDVKS LMRAAAQLLK SGHIQTGGST
ITMQVAKNYF LTNERSFSRK INEILLALQI ERQLTKDEIL ELYVNKIYLG NRAYGIEAAA
QVYYGKPIKD LSLAEMAMIA GLPKAPSRYN PLVNPTRSTE RRNWILERML KLGFIDQQRY
QAAVEEPINA SYHVQTPELN APYIAEMARA EMVGRYGSEA YTEGYKVITT VRSDLQNAAS
QSVRDGLIDY DQRHGYRGPE TRLPGQTRDA WLKHLGQQRS IGGLEPAIVT QVEKSGIMVM
TRDGKEEAVT WDSMKWARPF LSNNSMGPMP RQPADVAQAG DQIRVQRQED GTLRFVQIPA
AQSALISLDP KDGAIRSLVG GFSFEQSNYN RAIQAKRQPG SSFKPFIYSA ALDNGFTAAS
LVNDAPIVFV DEYLDKVWRP KNDTNTFLGP IPLREALYKS RNMVSIRVLQ GLGIERAISY
ITKFGFQRDE LPRNFSLALG TATVTPMEIA GAWSVFANGG YKVNPYVIER IESRDGQVLY
QANPPRVPVE EQVAADAEDA GNPGDPEHPE SAEGEGSIEA QQVAAKAQTT FEPTPAERII
DARTAYIMTS MLQDVIKRGT GRRALALKRT DLAGKTGTTN DSKDGWFSGY NSDYVTSVWV
GFDQPETLGR REYGGTVALP IWIRYMGFAL KDKPMHTMAE PPGIVSLRID PVTGRSAAPG
TPGAYFEMFK NEDTPPSVNE LPPGSFPGSP LPDDEGAPID LF
