ID   A5YIK8_STREE            Unreviewed;       729 AA.
AC   A5YIK8;
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:ABR04061.1};
DE   Flags: Fragment;
GN   Name=pbp2x {ECO:0000313|EMBL:ABR04061.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:ABR04061.1};
RN   [1] {ECO:0000313|EMBL:ABR04061.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=685.6PL97 {ECO:0000313|EMBL:ABR04061.1};
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; EF501687; ABR04061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5YIK8; -.
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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 2.
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:ABR04061.1"
SQ   SEQUENCE   729 AA;  79991 MW;  2D55F3A45BBD3987 CRC64;
     RRRVGKSLSL LSVFVFAIFL VNFAVIIGTG TRFGTDLAKE AKKVHQTTRT VPAKRGTIYD
     RNGVPIAEDA TSYNVYAVID KKYKSATGKI LYVEDSQFNK VAEVFHKYLD MDEAYVKEQL
     SQPNLTQVSF GAKGNGITYA NMMAIKKDLK DASVEGIDFT TSPNRSYPNG QFTSSFIGLA
     QLHENEDGSK SLLGTSGMES SLNSILAGKD GIITYEKDRL GNIVPGTEQI SQKTVNGKDV
     YTTISSTLQS FMETQMDAFQ EKLKGKYMTA TLVSAKTGEI LATTQRPTFN ADTKEGITED
     FVWRDILYQS NYEPGSAFKV MTLASSIDNN TFPSGEYFNS SEFKIADATT RDWDVNAGLT
     TGGMMTFLQG FAHSSNVGTS LLEQKMGDAT WLDYLKRFKF GVPTRFGLTD EYAGQLPADN
     IVSIAQSSFG QGISVTQTQM LRAFTAIAND GVMLEPKFIS AIYDTNNQSV RKSQKEIVGN
     PVSKEAASTT RNHMILVGTD PLYGTMYNHY TGKPIITVPG QNVALKSGTA QIADEKNGGY
     LVGTTDYIFS AVSMNPAENP DFILYVTVQQ PEHFSGIQLG EFATPILERA SAMKESLNLQ
     SPAKNLDQVT TESSYAMPSI KDISPGELAE ALRRNIVQPI VVGTGTKIKE TSVEEGKNLA
     PNQQVLLLSD KVEEIPDMYG WKKETAETFA KWLDIELEFE GSGSIVQKQD VRTNTAIKNI
     KKIKLTLGD
//