ID B2Y3W2_STREE Unreviewed; 592 AA.
AC B2Y3W2;
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:ACB14584.1};
DE Flags: Fragment;
GN Name=pbp2b {ECO:0000313|EMBL:ACB14584.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ACB14584.1};
RN [1] {ECO:0000313|EMBL:ACB14584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=595.7Oh00 {ECO:0000313|EMBL:ACB14584.1}, and 640.9Oh00
RC {ECO:0000313|EMBL:ACB14586.1};
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; EU378036; ACB14584.1; -; Genomic_DNA.
DR EMBL; EU378038; ACB14586.1; -; Genomic_DNA.
DR AlphaFoldDB; B2Y3W2; -.
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:ACB14584.1"
FT NON_TER 592
FT /evidence="ECO:0000313|EMBL:ACB14584.1"
SQ SEQUENCE 592 AA; 63554 MW; 7765F3230EB75B2B CRC64;
ASQTKVTTSS ARGEIYDASG KPLVENTLKQ VVSFTRSNKM TATDLKEIAK KLLTYVSISS
PNLTERQLAD YYLADPEIYK KTVEALPSEK RLDSDGNRLS ESELYNNAVD SVPTSQLNYT
EDEKKEIYLF SQLNAVGNFA TGTIATDPLN DSQVAVIASI SKEMPGISIS TSWDRKVLET
SLSSIVGSVS SEKAGLPAEE VDTYLKKGYS LNDRVGTSYL EKQYEETLQG KRSVKEIHLD
KYGNMESVDT IEEGSKGNNI KLTIDLAFQD SVDALLKSYF NSELGNGGAK YSEGVYAVAL
NPKTGAVLSM SGLKHDLNTG ELTPDSLGTV TNVFVPGSVV KAATISSGWE NGVLSGNQTL
TDQPIVFQGS APIYSWYKLA YGSFPITAVE ALEYSSNAYM VQTALGIMGQ TYQPNMFVGT
SNLETAMGKL RATFGEYGLG AATGIDLPDE STGFVPKEYS FANYITNAFG QFDNYTPMQL
AQYVATIAND GVRVAPRIVE GIYGNNDKGG LGELIQAIDT KEINKVNISE SDMAILHQGF
YQVSHGTSPL TTGRAFSDGA TVSISGKTGT GESYVAGGQE ANNTNAVAYA PS
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