ID A0A2X3W718_9STRE Unreviewed; 747 AA.
AC A0A2X3W718;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Penicillin-binding protein 2X {ECO:0000313|EMBL:SQF39563.1};
GN Name=pbpX {ECO:0000313|EMBL:SQF39563.1};
GN ORFNames=NCTC12278_00418 {ECO:0000313|EMBL:SQF39563.1};
OS Streptococcus ferus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1345 {ECO:0000313|EMBL:SQF39563.1, ECO:0000313|Proteomes:UP000249495};
RN [1] {ECO:0000313|EMBL:SQF39563.1, ECO:0000313|Proteomes:UP000249495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12278 {ECO:0000313|EMBL:SQF39563.1,
RC ECO:0000313|Proteomes:UP000249495};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483343; SQF39563.1; -; Genomic_DNA.
DR RefSeq; WP_018030930.1; NZ_LS483343.1.
DR AlphaFoldDB; A0A2X3W718; -.
DR STRING; 1123303.GCA_000372425_01617; -.
DR KEGG; sfer:NCTC12278_00418; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000249495; Chromosome 1.
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; cd06576; PASTA_Pbp2x-like_1; 1.
DR CDD; cd06575; PASTA_Pbp2x-like_2; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000249495};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 628..688
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 690..747
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 747 AA; 81723 MW; 0184BBCF0D785139 CRC64;
MRTFMKSFLD YVVGDRRTPQ KNRERVGQNL MILSVFIFFV FIINFIIIIG SDSKFGVDLS
KGASSVYQTV HTVQARRGTI YDRNGNPIAE DSTTYSIYAV INKSYVSTSG EKLYVQSSQF
DQVADIFSQH LGMDKNYVLS QLKQKKLSQV SFGTQGSNIS YSTMTTVKDA LASAHINGVD
FTTSPGRMYP NGVFASQFIG LAQVKENKDG TKSLVGATGM EASLDAILSG KDGQVTYQKD
KNGNTLLGTA TTIKKAENGK DVYTTLSAPI QTYLERQMDI FQEKAKGVQA SATLVNAKTG
EILATTQRPS FDSDTKAGLD AEGFTWQNVL YQTNYEPGST MKVMTLASAI DKGVFNPNEA
YDSSGLTIAD ATIKDWDVNE GLTTGQYLTY AQGFAHSSNV GMTYLEQKMG NETWLNYLNK
FRFGFPTRFG MGSEASGLLP SDNIVTIAMS SFGQGIGVTQ TQMLRAFSAI SNDGVMLEPQ
FISKIYDPNT DTSRSAKKEV VGNPVSKKAA TETRQYMVTV GTDPYYGTLN SNGSPVIQVG
NQSVAVKSGT AQIAAEDGSG YLTGSHDYIY SVVAMVPSEN PDFMMYVTLQ QPESFSMTYW
QDVVNPVLEE ATLMKDTLLE PAANPLKSQT KFAMPDIVGK SPGDSADQLR QNLVQPIILG
SGSKITKTSV AKGKNLKENQ QILLLTSNFE TVPDMYGWTK KNVETFAKWT NIKITYKGQK
SGRVTKQNVE VGKKLNSIKK MTITLGE
//
