ID Q83XA7_STREE Unreviewed; 702 AA.
AC Q83XA7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Penicillin-binding protein 2x {ECO:0000313|EMBL:CAD90771.2};
DE Flags: Fragment;
GN Name=pbp2x {ECO:0000313|EMBL:CAD90771.2};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:CAD90771.2};
RN [1] {ECO:0000313|EMBL:CAD90771.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=5204 {ECO:0000313|EMBL:CAD90771.2};
RX PubMed=12923202; DOI=10.1074/jbc.M305948200;
RA Chesnel L., Pernot L., Lemaire D., Champelovier D., Croize J., Dideberg O.,
RA Vernet T., Zapun A.;
RT "The structural modifications induced by the M339F substitution in PBP2x
RT from Streptococcus pneumoniae further decreases the susceptibility to beta-
RT lactams of resistant strains.";
RL J. Biol. Chem. 278:44448-44456(2003).
RN [2] {ECO:0000313|EMBL:CAD90771.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=5204 {ECO:0000313|EMBL:CAD90771.2};
RA Chesnel L.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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; AJ560762; CAD90771.2; -; Genomic_DNA.
DR AlphaFoldDB; Q83XA7; -.
DR SMR; Q83XA7; -.
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; -; 2.
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 584..643
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 644..702
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAD90771.2"
SQ SEQUENCE 702 AA; 76969 MW; BFF3C78D348227A3 CRC64;
GTGTRFGTDL AKEAKKVHQT TRTVPAKRGT IYDRNGVPIA EDATSYNVYA VIDENYKSAT
GKILYVEKTQ FNKVAEVFHK YLDMEESYVR EQLSQPNLKQ VSFGAKGNGI TYANMMAIKK
DLKDASVEGI DFTTSPNRSY PNGQFASSFI GLAQLHENED GSKSLLGTSG MESSLNSILA
GKDGIITYEK DRLGNIVPGT EQVSQQTVDG KDVYTTLSSP LQSFMETQMD AFLEKVKGKY
MTATLVSAKT GEILATTQRP TFNADTKEGI TEDFVWRDIL YQSNYEPGSA FKVMMLASSI
DNNTFPSGEY FNSSEFKIAD ATTRDWDVNA GLTTGGMMTF LQGFAHSSNV GTSLLEQKMG
DATWLDYLKR FKFGVPTRFG LTDEYAGQLP ADNIVSIAQS SFGQGISVTQ TQMLRAFTAI
ANDGVMLEPK FISAIYDTNN QSVRKSQKEI VGNPVSKEAA STTRNHMILV GTDPLYGTMY
NHYTGKPIIT VPGQNVAVKS GTAQIADEKN GGYLVGSTNY IFSVVTMNPA ENPDFILYVT
VQQPEHFSGI QLGEFATPIL ERASAMKESL NLQSPAKNLD KVTTESSYAM PSIKDISPGE
LAEALRRNIV QPIVVGTGTK IKETSVEEGT NLAPNQQVLL LSDKVEEIPD MYGWKKETAE
TFAKWLDIEL EFEGSGSVVQ KQDVRTNTAI KNIKKIKLTL GD
//
