ID Q4TUL4_STREE Unreviewed; 670 AA.
AC Q4TUL4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Penicillin-binding protein 2X {ECO:0000313|EMBL:AAY56852.1};
DE Flags: Fragment;
GN Name=pbp2x {ECO:0000313|EMBL:AAY56852.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:AAY56852.1};
RN [1] {ECO:0000313|EMBL:AAY56852.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 51916 {ECO:0000313|EMBL:AAY56852.1};
RA Dib-Hajj F., Gootz T., Kaczmarek F., Shang W., Cronan M.;
RT "Sequence analysis of pbp2x, pbp2b, pbp1a and murMN genes from a reference
RT set of Streptococcus pneumoniae resistant to beta-lactams.";
RL Submitted (MAY-2005) 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; DQ056808; AAY56852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4TUL4; -.
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 552..611
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 612..670
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY56852.1"
SQ SEQUENCE 670 AA; 73545 MW; 362A5BB08DD3A966 CRC64;
DRNGVPIAED ATSYNVYAVI DENYKSATGK ILYVEKTQFN KVAEVFHKYL DMEESYVREQ
LSQPNLKQVS FGAKGNGITY ANMMTIKKEL ETAEVKGIDF TTSPNRSYPN GQFASSFIGL
AQLHENEDGS KSLLGTSGME SSLNSILAGT DGIITYEKDR LGNIVPGTEL VSQQTVDGKD
VYTTLSSPLQ SFMETQMDAF LEKVKGKYMT ATLVSAKTGE ILATTQRPTF NADTKEGITE
DFVWRDILYQ SNYEPGSAFK VMMLASSIDN NTFPSGEYFN SSEFKIADAT TRDWDVNEGL
TTGGMMTFSQ GFAHSSNVGT SLLEQKMGDA TWLDYLKRFK FGVPTRFGLT DEYAGQLPAD
NIVSIAQSSF GQGISVTQTQ MLRAFTAIAN DGVMLEPKFI SAIYDTNNQS VRKSQKEIVG
NPVSKEAAST TRNHMILVGT DPLYGTMYNH YTGKPIITVP GQNVAVKSGA AQIADEKNGG
YLVGSTNYIF SVVTMNPAEN PDFILYVTVQ QPEHYSGIQL GEFATPILER ASAMKESLNL
QSPAKNLDKV TTESSYAMPS IKDISPGELA EALRRNIVQP IVVGTGTKIK ETSVEEGTNL
APNQQVLLLS DKVEEIPDMY GWKKETAETF AKWLDIELEF EGSGSVVQKQ DVRTNTAIKN
IKKIKLTLGD
//
