ID B5LNZ1_STREE Unreviewed; 458 AA.
AC B5LNZ1;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Penicillin-binding protein 2B {ECO:0000313|EMBL:ACG50834.1};
DE Flags: Fragment;
GN Name=pbp2B {ECO:0000313|EMBL:ACG50834.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ACG50834.1};
RN [1] {ECO:0000313|EMBL:ACG50834.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMC24 {ECO:0000313|EMBL:ACG50834.1};
RA Kosowska-Shick K.M., McGhee P.L., Appelbaum P.C.;
RT "Amino acid alterations in penicillin-binding proteins (PBP) 1A, 2B, and 2X
RT and murein in 31 clinical isolates with vary beta-lactam pneumococci.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACG50834.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMC24 {ECO:0000313|EMBL:ACG50834.1};
RX PubMed=19237649; DOI=10.1128/AAC.01566-08;
RA Kosowska-Shick K., McGhee P., Appelbaum P.C.;
RT "Binding of faropenem and other beta-lactam agents to penicillin-binding
RT proteins of pneumococci with various beta-lactam susceptibilities.";
RL Antimicrob. Agents Chemother. 53:2176-2180(2009).
RN [3] {ECO:0000313|EMBL:ACG50834.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMC24 {ECO:0000313|EMBL:ACG50834.1};
RX PubMed=19307366; DOI=10.1128/AAC.01531-08;
RA Kosowska-Shick K., Ednie L.M., McGhee P., Appelbaum P.C.;
RT "Comparative antipneumococcal activities of sulopenem and other drugs.";
RL Antimicrob. Agents Chemother. 53:2239-2247(2009).
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; EU863659; ACG50834.1; -; Genomic_DNA.
DR AlphaFoldDB; B5LNZ1; -.
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 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 1..82
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 131..457
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACG50834.1"
FT NON_TER 458
FT /evidence="ECO:0000313|EMBL:ACG50834.1"
SQ SEQUENCE 458 AA; 48722 MW; AE82F0DC2961AE4B CRC64;
GISISTSWDR KVLETSLSSI VGSVSSEKAG LPAEEAEAYL KKGYSLNDRV GTSYLEKQYE
ETLQGKRSVK EIHLDKYGNM ESVDTIEEGS KGNNIKLTID LAFQDSVDAL LKSYFNSELG
NGGAKYSEGV YAVALNPKTG AVLSMSGIKH DLKTGELTPD SLGTVTNVFV PGSVVKAATI
SSGWENGVLS GNQTLTDQSI VFQGSAPINS WYPAFSRPMP ITAVQALEYS SNAYMVQTAL
GLMGQTYQPN MFVGTSNLES AMGKLRSTFG EYGLGSATGI DLPDESTGFV PKEYSFANFI
TNAFGQFDNY TPMQLAQYVA TIANDGVRVA PRIVEGIYGN NDKGGLGDLI QQLQPTEMNK
VNISDSDMSI LHQGFYQVAH GTSELTTGRA FSNGALVSIS GKTGTAESYV ADGQQATNTN
AVAYAPSDNP QIAVAVVFPH NTNLTNGVGP SIARDIIN
//
