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Database: UniProt
Entry: A0A1G8T4Q1_9BURK
LinkDB: A0A1G8T4Q1_9BURK
Original site: A0A1G8T4Q1_9BURK 
ID   A0A1G8T4Q1_9BURK        Unreviewed;       422 AA.
AC   A0A1G8T4Q1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Transglycosylase {ECO:0000313|EMBL:SDJ36381.1};
GN   ORFNames=SAMN05444748_11316 {ECO:0000313|EMBL:SDJ36381.1};
OS   Variovorax sp. OV700.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDJ36381.1, ECO:0000313|Proteomes:UP000199505};
RN   [1] {ECO:0000313|Proteomes:UP000199505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; FNDR01000013; SDJ36381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8T4Q1; -.
DR   STRING; 1882826.SAMN05444748_11316; -.
DR   OrthoDB; 8835701at2; -.
DR   Proteomes; UP000199505; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          241..379
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
SQ   SEQUENCE   422 AA;  45550 MW;  C7C9E7609B4D393F CRC64;
     MNKILRFVIY ALSALVVTAC LAVFLIVKFA LAPAPGEWST SVKAGPLSFQ VGVPAAVRLA
     TSSWLAPRLD GHSVETRFGT VRFAWKAADG LLELRCAPCS LEVAALGTQP IQVEGLVATV
     RRDGNTLAGT LTATPRNADA AAVIQGPWEG RLAPKGLHFS ADIKDAPIAR WYAVLAPHLP
     ELQRSRIGGT LAVRAQVALP EGTFVVLPSV SQFTVEGLGT EAMLGARTSC GAPSKLANDS
     WLARAVIAAE DQRFFTHAGY DLTEIVASID NNQKDGQQKR GASTLTQQLA KMLVTGSDRT
     AERKLRELLY AVEMEQTLGK ARILQLYLDN APWGGNLCGA EAAARRYFKR PARNLEPAQA
     VWLAAMLHKP QAVLEQWRHD GRIDPDRTKW VAEGVRGISR NQREALLKSV AAARFTAPEA
     VP
//
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