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Database: UniProt
Entry: A5YI04_STREE
LinkDB: A5YI04_STREE
Original site: A5YI04_STREE 
ID   A5YI04_STREE            Unreviewed;       732 AA.
AC   A5YI04;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Penicillin-binding protein 2x {ECO:0000313|EMBL:ABR03857.1};
DE   Flags: Fragment;
GN   Name=pbp2x {ECO:0000313|EMBL:ABR03857.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:ABR03857.1};
RN   [1] {ECO:0000313|EMBL:ABR03857.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=0.10FR96 {ECO:0000313|EMBL:ABR03857.1}, 0.56SW00
RC   {ECO:0000313|EMBL:ABR03879.1}, and 595.6SP00
RC   {ECO:0000313|EMBL:ABR04008.1};
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; EF501483; ABR03857.1; -; Genomic_DNA.
DR   EMBL; EF501505; ABR03879.1; -; Genomic_DNA.
DR   EMBL; EF501634; ABR04008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5YI04; -.
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; 2.
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; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 1.
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          614..673
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          674..732
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABR03857.1"
SQ   SEQUENCE   732 AA;  80097 MW;  B4B21E32B16396A0 CRC64;
     AENRRRVGKS LSLLSVFVFA IFLVNFAVII GTGTRFGTDL AKEAKKVHQT TRTVPAKRGT
     IYDRNGVPIA EDATSYNVYA VIDENYKSAT GKILYVEKTQ FNKVAEVFHK YLDMEESYVR
     EQLSQPNLKQ VSFGAKGNGI TYANMMSIKK ELEAAEVKGI DFTTSPNRSY PNGQFASSFI
     GLAQLHENED GSKSLLGTSG MESSLNSILA GTDGIITYEK DRLGNIVPGT EQVSQRTMDG
     KDVYTTISSP LQSFMETQMD AFQEKVKGKY MTATLVSAKT GEILATTQRP TFDADTKEGI
     TEDFVWRDIL YQSNYEPGST MKVMMLAAAI DNNTFPGGEV FNSSELKIAD ATIRDWDVNE
     GLTGGRMMTF SQGFAHSSNV GMTLLEQKMG DATWLDYLNR FKFGVPTRFG LTDEYAGQLP
     ADNIVNIAQS SFGQGISVTQ TQMIRAFTAI ANDGVMLEPK FISAIYDPND QTARKSQKEI
     VGNPVSKDAA SLTRTNMVLV GTDPVYGTMY NHSTGKPTVT VPGQNVALKS GTAQIADEKN
     GGYLVGLTDY IFSAVSMSPA ENPDFILYVT VQQPEHYSGI QLGEFANPIL ERASAMKDSL
     NLQTTAKALE QVSQQSPYPM PSVKDISPGD LAEELRRNLV QPIVVGTGTK IKNSSAEEGK
     NLAPNQQVLI LSDKAEEVPD MYGWTKETAE TLAKWLNIEL EFQGSGSTVQ KQDVRANTAI
     KDIKKITLTL GD
//
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