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Database: UniProt
Entry: A5YIF2_STREE
LinkDB: A5YIF2_STREE
Original site: A5YIF2_STREE 
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
//
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