PBP2_STRPN
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 25-MAY-2022, entry version 98.
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; Firmicutes; 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 RefSeq; WP_001224867.1; NC_003028.3.
DR AlphaFoldDB; P0A3M5; -.
DR SMR; P0A3M5; -.
DR STRING; 170187.SP_1673; -.
DR BindingDB; P0A3M5; -.
DR ChEMBL; CHEMBL1255133; -.
DR DrugBank; DB01150; Cefprozil.
DR DrugBank; DB05659; Faropenem medoxomil.
DR MEROPS; X52.001; -.
DR EnsemblBacteria; AAK75752; AAK75752; SP_1673.
DR KEGG; spn:SP_1673; -.
DR eggNOG; COG0768; Bacteria.
DR OMA; TLACKTG; -.
DR PhylomeDB; P0A3M5; -.
DR BRENDA; 2.4.1.129; 1960.
DR PRO; PR:P0A3M5; -.
DR Proteomes; UP000000585; 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: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; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW 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
