ID Q9RCR3_STREE Unreviewed; 666 AA.
AC Q9RCR3;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Penicillin binding protein 2x {ECO:0000313|EMBL:CAB65446.1};
DE Flags: Fragment;
GN Name=pbp2x {ECO:0000313|EMBL:CAB65446.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:CAB65446.1};
RN [1] {ECO:0000313|EMBL:CAB65446.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F1 {ECO:0000313|EMBL:CAB65446.1};
RA Hakenbeck R.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAB65446.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F1 {ECO:0000313|EMBL:CAB65446.1};
RA Koenig A., Reinhardt R., Regine H.;
RT "Mosaic structure of pbp2x genes in penicillin resistant clones of
RT Streptococcus pneumoniae.";
RL Submitted (JAN-2000) 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; AJ238585; CAB65446.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RCR3; -.
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; 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 548..607
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 608..666
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB65446.1"
FT NON_TER 666
FT /evidence="ECO:0000313|EMBL:CAB65446.1"
SQ SEQUENCE 666 AA; 73027 MW; E92F275307D40111 CRC64;
VPIAEDATSY NVYAVIDENY KSATGKILYV EKTQFNKVAE VFHKYLDMEE SYVREQLSQP
NLKQVSFGSK GNGITYANMM AIKKELETAE VKGIDFTTSP NRSYPNGQFA SSFIGLAQLH
ENEDGSKSLL GTSGMESSLN SILAGTDGII TYEKDRLGNI VPGTEQVSQQ TVDGKDVYTT
ISSPLQSFME TQMDAFREKV KGKYMTATLV SAKTGEILAT TQRPTFDADT KEGITEDFVW
RDILYQSNYE PGSAMKVMML AAAIDNNTFP GGEVFNSSEL KIADVTIRDW NVNEGLTGGR
MMTFSQGFAH SSNVGMTLLE QKMGDATWLD YLNRFKFGVS TRFGLTDEYA GQLPADNIVN
IAQSSFGQGI SVTQTQMIRA FTAIANDGVM LEPKFITALY DPNNQTVRRS QKEIVGNPVS
KDAAGQTRTH MVLVGTDPRY GTMYNHSTGK ATVNVPGQNV ALKSGTAEIA DEKNGGYLVG
STNNIFSVVA MNPAENPDFI LYVTVQQPEH YSGIQLGEFA NPILERASAM KESLNLQSPA
KNLDKVTTES SYAMPSIKDI SPGELAEALR RNIVQPIVVG TGTKIKETSV EEGTNLAPNQ
QVLLLSDKVE EIPDMYGWKK ETAETFAKWL DIELEFEGSG SVVQKQDVRT NTAIKNIKKI
KLTLGD
//
