ID   PBP2_STRPN              Reviewed;         680 AA.
AC   P0A3M5; P10524;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Penicillin-binding protein 2B;
DE            Short=PBP2b;
GN   Name=penA {ECO:0000303|PubMed:2654541}; Synonyms=pbp2b;
GN   OrderedLocusNames=SP_1673;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-680.
RC   STRAIN=64147;
RX   PubMed=2654541; DOI=10.1111/j.1365-2958.1989.tb00108.x;
RA   Dowson C.G., Hutchison A., Spratt B.G.;
RT   "Extensive re-modelling of the transpeptidase domain of penicillin-binding
RT   protein 2B of a penicillin-resistant South African isolate of Streptococcus
RT   pneumoniae.";
RL   Mol. Microbiol. 3:95-102(1989).
CC   -!- FUNCTION: A transpeptidase that forms peptide cross-links between
CC       adjacent glycan strands in cell wall peptidoglycan (PG). Part of the
CC       elongasome machinery that synthesizes peripheral PG.
CC       {ECO:0000250|UniProtKB:A0A0H2ZQ75}.
CC   -!- SUBUNIT: Interacts with MreC in the elongasome.
CC       {ECO:0000250|UniProtKB:P0A3M6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}. Note=Localizes to the midcell division sites,
CC       colocalizes with StkP. {ECO:0000250|UniProtKB:A0A0H2ZQ75}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; AE005672; AAK75752.1; -; Genomic_DNA.
DR   EMBL; X13136; CAA31526.1; -; Genomic_DNA.
DR   PIR; B35965; B35965.
DR   PIR; G95194; G95194.
DR   AlphaFoldDB; P0A3M5; -.
DR   SMR; P0A3M5; -.
DR   BindingDB; P0A3M5; -.
DR   ChEMBL; CHEMBL1255133; -.
DR   DrugBank; DB01150; Cefprozil.
DR   DrugBank; DB05659; Faropenem medoxomil.
DR   MEROPS; X52.001; -.
DR   PaxDb; 170187-SP_1673; -.
DR   EnsemblBacteria; AAK75752; AAK75752; SP_1673.
DR   KEGG; spn:SP_1673; -.
DR   eggNOG; COG0768; Bacteria.
DR   PhylomeDB; P0A3M5; -.
DR   BRENDA; 2.4.1.129; 1960.
DR   PRO; PR:P0A3M5; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IEA:InterPro.
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   Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR047982; PBP2B.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; NF038278; strep_PBP2B; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..680
FT                   /note="Penicillin-binding protein 2B"
FT                   /id="PRO_0000195455"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        386
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
FT   VARIANT         333
FT                   /note="E -> G (in strain: 64147)"
FT   VARIANT         426..432
FT                   /note="TQAYGSF -> PAFSRPM (in strain: 64147)"
FT   VARIANT         446
FT                   /note="T -> A (in strain: 64147)"
FT   VARIANT         476
FT                   /note="E -> G (in strain: 64147)"
FT   VARIANT         489
FT                   /note="T -> S (in strain: 64147)"
FT   VARIANT         512
FT                   /note="Y -> F (in strain: 64147)"
FT   VARIANT         538
FT                   /note="N -> D (in strain: 64147)"
FT   VARIANT         597
FT                   /note="G -> E (in strain: 64147)"
FT   VARIANT         674..676
FT                   /note="QKY -> NQH (in strain: 64147)"
SQ   SEQUENCE   680 AA;  73873 MW;  56BF2C1AA9B54C3B CRC64;
     MRKFNSHSIP IRLNLLFSIV ILLFMTIIGR LLYMQVLNKD FYEKKLASAS QTKITSSSAR
     GEIYDASGKP LVENTLKQVV SFTRSNKMTA TDLKETAKKL LTYVSISSPN LTERQLADYY
     LADPEIYKKI VEALPSEKRL DSDGNRLSES ELYNNAVDSV QTSQLNYTED EKKEIYLFSQ
     LNAVGNFATG TIATDPLNDS QVAVIASISK EMPGISISTS WDRKVLETSL SSIVGSVSSE
     KAGLPAEEAE AYLKKGYSLN DRVGTSYLEK QYEETLQGKR SVKEIHLDKY GNMESVDTIE
     EGSKGNNIKL TIDLAFQDSV DALLKSYFNS ELENGGAKYS EGVYAVALNP KTGAVLSMSG
     IKHDLKTGEL TPDSLGTVTN VFVPGSVVKA ATISSGWENG VLSGNQTLTD QSIVFQGSAP
     INSWYTQAYG SFPITAVQAL EYSSNTYMVQ TALGLMGQTY QPNMFVGTSN LESAMEKLRS
     TFGEYGLGTA TGIDLPDEST GFVPKEYSFA NYITNAFGQF DNYTPMQLAQ YVATIANNGV
     RVAPRIVEGI YGNNDKGGLG DLIQQLQPTE MNKVNISDSD MSILHQGFYQ VAHGTSGLTT
     GRAFSNGALV SISGKTGTAE SYVADGQQAT NTNAVAYAPS DNPQIAVAVV FPHNTNLTNG
     VGPSIARDII NLYQKYHPMN
//