ID A0A264W1W9_9BACL Unreviewed; 670 AA.
AC A0A264W1W9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:OZS77555.1};
GN ORFNames=CF394_10090 {ECO:0000313|EMBL:OZS77555.1};
OS Tetzosporium hominis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Tetzosporium.
OX NCBI_TaxID=2020506 {ECO:0000313|EMBL:OZS77555.1, ECO:0000313|Proteomes:UP000217065};
RN [1] {ECO:0000313|EMBL:OZS77555.1, ECO:0000313|Proteomes:UP000217065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-49 {ECO:0000313|EMBL:OZS77555.1,
RC ECO:0000313|Proteomes:UP000217065};
RA Tetz G., Tetz V.;
RT "Tetzosporium hominis gen.nov. sp.nov.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZS77555.1}.
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DR EMBL; NOKQ01000220; OZS77555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264W1W9; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000217065; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000217065};
KW Transferase {ECO:0000313|EMBL:OZS77555.1}.
FT DOMAIN 24..148
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 158..309
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 354..665
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 670 AA; 73603 MW; CD7BE2F8E3A80847 CRC64;
MKKWGWGVLA VPLLVLAGCN DEVTPQERQE AYVAAWNEGD YETLYNEFVS DETKEQVDEA
AFVERQVALD EALGVTEREV TFTKAPEDAQ WEAAEPATFP VQIKVETVAG PVEWEKEMTW
QSVETDEELT WMADWDTGFI LPDLAEGDEV RVSTLPFARG EIYDRNGNAL AINGTGFEVG
IVPGKFTDDA QKPRLAELLG TTVEYIDKQL AQSWVKDDQF VPIDKIAQTD DVRAALLEIP
GVLLQETAMR EYPYGEAAAH LVGYIGPITA EQLAEREDEG YTEFDQIGRQ GLESFLEERL
RGQDGKRVFI DKAEEGLENV MLAEKEPVAG ERIDLTIDAE LQRITFASMD GEPGAAAVVD
PKTGEVLTLL SSPSFDPSAF MLGMTQAQYD ELANDPLNPL LNRFAASYAP GSTLKPITAA
IGMEAGTLDP TEGIVIEGAT WQKDDSWGDY RVTRLHPEAP NPIDLEKSLV YSDNIYYAQQ
ALKMGRETFV EGLESFGFGE DIPFFLNLQA SQVSNDGGIG SEGQLADTSF GQGQMLANIL
HLASSYQPFL TNGTMWQPTL LLEEDDQVVW KEGLVSEQNA AILQEGMRSM VVDGFAQAAN
IPNIPLAGKT GTAELKATID AEGQENGFFV SYPVDTEEMI MAMMIEDVGD NNGSGYVAEK
AAAIYKLLYE
//
