ID   B2Y3R8_STREE            Unreviewed;       592 AA.
AC   B2Y3R8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Penicillin binding protein 2b {ECO:0000313|EMBL:ACB14540.1};
DE   Flags: Fragment;
GN   Name=pbp2b {ECO:0000313|EMBL:ACB14540.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:ACB14540.1};
RN   [1] {ECO:0000313|EMBL:ACB14540.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=125.1Oh97 {ECO:0000313|EMBL:ACB14540.1};
RX   PubMed=18394970; DOI=10.1016/j.meegid.2008.02.001;
RA   Stanhope M.J., Lefebure T., Walsh S.L., Becker J.A., Lang P.,
RA   Pavinski Bitar P.D., Miller L.A., Italia M.J., Amrine-Madsen H.;
RT   "Positive selection in penicillin-binding proteins 1a, 2b, and 2x from
RT   Streptococcus pneumoniae and its correlation with amoxicillin resistance
RT   development.";
RL   Infect. Genet. Evol. 8:331-339(2008).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; EU377992; ACB14540.1; -; Genomic_DNA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
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   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          9..247
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          296..591
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACB14540.1"
FT   NON_TER         592
FT                   /evidence="ECO:0000313|EMBL:ACB14540.1"
SQ   SEQUENCE   592 AA;  63732 MW;  07439AD84C18370E CRC64;
     ASQTKITSSS ARGEIYDASG KPLVENTLKQ VVSFTRSNKM TATDLKETAK KLLTYVSISS
     PNLTERQLAD YYLADPEIYK KIVEALPSEK RLDSDGNRLS ESXLYNNAVD SVQTSQLNYT
     EDEKKEIYLF XQLNAVGNFA TGTIATDPLN DSQVAVIASI SKEMPGISIS TSWDRKVLET
     SLSSIVGSVS SEKAGLPAEE AEAYLKKGYS LNDRVGTSYL EKQYEETLQG KRSVKEIHLD
     KYGNMESVDT IEEGSKGNNI KLTIDLAFQD SVDALLKSYF NSELENGGAK YSEGVYAVAL
     NPKTGAVLSM SGIKHDLKTG ELTPDSLGTV TNVFVPGSVV KAATISSGWE NGVLSGNQTL
     TDQPIVFQGS APIYSWYKLA YGSFPITAVE ALEYSSNAYM VQTALGIMGQ TYQPNMFVXT
     SNLETAMGKL RATFGEYGLG AATGIDLPDE STGFVPKEYS FANYITNAFG QFDNYTPMQL
     AQYVATIAND GVRVAPRIVE GIYGNNDKGG LGDLIQQLQP TEMNKVNISD SDMSVLHQGF
     YQVAHGTSGL TTGRAFSNGA LVSISGKTGT AESYVADGQQ ATNTNAVAYA PS
//