ID   PBP_STAAU               Reviewed;         670 AA.
AC   P07944;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-MAY-2023, entry version 104.
DE   RecName: Full=Beta-lactam-inducible penicillin-binding protein;
GN   Name=pbp;
OS   Staphylococcus aureus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3305073; DOI=10.1016/0014-5793(87)80373-3;
RA   Song M.D., Wachi M., Doi M., Ishino F., Matsuhashi M.;
RT   "Evolution of an inducible penicillin-target protein in methicillin-
RT   resistant Staphylococcus aureus by gene fusion.";
RL   FEBS Lett. 221:167-171(1987).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: In the presence of beta-lactam antibiotics, MRSA cells
CC       produce this unique PBP in excessively large amounts and can still
CC       proliferate, while all the normal PBPs are inactivated (reversible
CC       switching ability of PBP formation).
CC   -!- MISCELLANEOUS: PBP has extremely low affinity to penicillin and most
CC       other beta-lactam antibiotics.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; Y00688; CAA68684.1; -; Genomic_DNA.
DR   AlphaFoldDB; P07944; -.
DR   SMR; P07944; -.
DR   DrugBank; DB02443; Methicillin Acyl-Serine.
DR   DrugBank; DB04041; Nitrocefin Acyl-Serine.
DR   DrugBank; DB02968; Penicillin G Acyl-Serine.
DR   DrugCentral; P07944; -.
DR   MEROPS; X52.001; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; 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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR007887; MecA_N.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell cycle; Cell division; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Membrane;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..670
FT                   /note="Beta-lactam-inducible penicillin-binding protein"
FT                   /id="PRO_0000195443"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        405
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
FT   BINDING         25
FT                   /ligand="a penicillin"
FT                   /ligand_id="ChEBI:CHEBI:51356"
FT                   /evidence="ECO:0000305"
FT   BINDING         405
FT                   /ligand="a penicillin"
FT                   /ligand_id="ChEBI:CHEBI:51356"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   670 AA;  76463 MW;  2DAA414D35DA993A CRC64;
     MKKIKIVPLI LIVVVVGFGI YFYASKDKEI NNTIDAIEDK NFKQVYKDSS YISKSDNGEV
     EMTERPIKIY NSLGVKDINI QDRKIKKVSK NKKRVDAQYK IKTNYGNIDR NVQFNFVKED
     GMWKLDWDHS VIIPGMQKDQ SIHIENLKSE RGKILDRNNV ELANTGTHMR LGIVPKNVSK
     KDYKAIAKEL SISEDYINNK WIKIGYKMIP SFHFKTVKKM DEYLSDFAKK FHLTTNETES
     RNYPLGKATS HLLGYVGPIN SEELKQKEYK GYKDDAVIGK KGLEKLYDKK LQHEDGYRVT
     IVRVDDNSNT IAHTLIEKKK KDGKDIQLTI DAKVQKSIYN NMKNDYGSGT AIHPQTGELL
     ALVSTPSYDV YPFMYGMSNE EYNKLTEDKK EPLLNKFQIT TSPGSTQKIL TAMIGLNNKT
     LDDKTSYKID GKGWQKDKSW GGYNVTRYEV VNGNIDLKQA IESSDNIFFA RVALELGSKK
     FEKGMKKLGV GEDIPSDYPF YNAQISNKNL DNEILLADSG YGQGEILINP VQILSIYSAL
     ENNGNINAPH LLKDTKNKVW KKNIISKENI NLLNDGMQQV VNKTHKEDIY RSYANLIGKS
     GTAELKMKQG ETGRQIGWFI SYDKDNPNMM MAINVKDVQD KGMASYNAKI SGKVYDELYE
     NGNKKYDIDE
//