ID Q30A55_STREE Unreviewed; 657 AA.
AC Q30A55;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Penicillin binding protein 2x {ECO:0000313|EMBL:ABB46509.1};
DE Flags: Fragment;
GN Name=pbp2x {ECO:0000313|EMBL:ABB46509.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ABB46509.1};
RN [1] {ECO:0000313|EMBL:ABB46509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=902 {ECO:0000313|EMBL:ABB46509.1};
RX PubMed=16586368; DOI=10.1086/501367;
RA Trzcinski K., Thompson C.M., Gilbey A.M., Dowson C.G., Lipsitch M.;
RT "Incremental increase in fitness cost with increased beta -lactam
RT resistance in pneumococci evaluated by competition in an infant rat nasal
RT colonization model.";
RL J. Infect. Dis. 193:1296-1303(2006).
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; DQ227582; ABB46509.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30A55; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd06573; PASTA; 1.
DR CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR Gene3D; 2.20.70.70; -; 1.
DR Gene3D; 3.30.70.2110; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; NF038271; strep_PBP2X; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03793; PASTA; 2.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR PROSITE; PS51178; PASTA; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 539..598
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 599..657
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABB46509.1"
SQ SEQUENCE 657 AA; 72205 MW; 25E87671783E975E CRC64;
YNVYAVIDEN YKSATGKILY VEKTQFNKVA EVFHKYLDME ESYVREQLSQ PNLKQVSFGS
KGNGITYANM MSIKKELETA EVKGIDFTTS PNRSYPNGQF ASSFIGLAQL HENEDGSKSL
LGTSGMESSL NSILAGTDGI ITYEKDRVGN IVPGTELVSQ QTVDGKDVYT TLSSPLQSFM
ETQMDAFLEK VKGKYMTATL VSAKTGEILA TTQRPTFNAD TKEGITEDFV WRDILYQSNY
EPGSAMKVMT LASSIDNNTF PSGEYFNSSE FKIADATTRD WDVNDGLTTG GMMTFLQGFA
HSSNVGMSLL EQKMGDATWL DYLKRFKFGV PTRFGLTDEY AGQLPADNIV SIAQSSFGQG
ISVTQTQMLR AFTAIANDGV MLEPKFISAI YDTNNQSVRK SQKEIVGNPV SKEAASTTRN
HMILVGTDPL YGTMYNHYTG KPIITVPGQN VAVKSGTAQI ADEKNGGYLV GSTNYIFSVV
TMNPAENPDF ILYVTVQQPE HYSGIQLGEF ATPILERASA MKESLNLQSP AKNLDKVTTE
SSYAMPSIKD ISPGELAEAL RRNIVQPIVV GTGTKIKETS VEEGTNLAPN QQVLLLSDKV
EEIPDMYGWK KETAETFAKW LDIELEFEGS GSVVQKQDVR TNTAIKNITK IKLTLGD
//
