ID A5YIF2_STREE Unreviewed; 729 AA.
AC A5YIF2;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Penicillin-binding protein 2x {ECO:0000313|EMBL:ABR04005.1};
DE Flags: Fragment;
GN Name=pbp2x {ECO:0000313|EMBL:ABR04005.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ABR04005.1};
RN [1] {ECO:0000313|EMBL:ABR04005.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=595.2FR99 {ECO:0000313|EMBL:ABR04005.1};
RX PubMed=17475572; DOI=10.1016/j.meegid.2007.03.004;
RA Stanhope M.J., Walsh S.L., Becker J.A., Miller L.A., Lefebure T., Lang P.,
RA Bitar P.D., Amrine-Madsen H.;
RT "The relative frequency of intraspecific lateral gene transfer of
RT penicillin binding proteins 1a, 2b, and 2x, in amoxicillin resistant
RT Streptococcus pneumoniae.";
RL Infect. Genet. Evol. 7:520-534(2007).
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; EF501631; ABR04005.1; -; Genomic_DNA.
DR AlphaFoldDB; A5YIF2; -.
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 611..670
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 671..729
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABR04005.1"
SQ SEQUENCE 729 AA; 79935 MW; 24BEF9F9535558B3 CRC64;
RRRVGKSLSL LSVFVFAVFL VNFAVIIGTG TRFGTDLAKE AKKVHQTTRT VPAKRGTIYD
RNGVPIAEDA TSYNVYAVID ENYKSATGKI LYVEKTQFNK VAEVFHKYLD MEESYVREQL
SQPNLKQVSF GSKGNGITYA NMMSIKKELE TAEVKGIDFT TSPNRSYPNG QFASSFIGLA
QLHENEDGSK SLLGTSGLES SLNTILAGTD GIITYEKDRV GNIVPGTELV SQQTVDGKDV
YTTLSSPLQS FMETQMDAFL EKVKGKYMTA TLVSAKTGEI LATTQRPTFN ADTKEGITKD
FVWRDILYQS NYEPGSAMKV MTLAAAIDNN TFPSGEYFNS SEFKIADATT RDWDVNAGLT
TGGMMTFLQG FAHSSNVGMS LLEQKMGDAT WLDYLKRFKF GVPTRFGLTD EYAGQLPADN
IVSIAQSSFG QGISVTQTQM LRAFTAIAND GVMLEPKFIS AIYDTNNQSV RKSQKEIVGN
PVPKEAASTT RNHMILVGTD PLYGTMYNHY TGKPIITVPG QNVAVKSGTA QIADEKNGGY
LVGSTNYIFS AVTMNPAENP DFILYVTVQQ PEHYSGIQLG EFATPILERA SAMKESLNLQ
SPAKNLDKVT TESSYAMPSI KDISPGELAE ALRRNIVQPI VVGTGTKIKE TSVEEGTNLA
PNQQVLLLSD KVEEIPDMYG WKKETAEAFA KWLDIELEFE GSGSVVQKQD VRTNTAIKNI
KKIKLTLGD
//