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Database: UniProt
Entry: B6ERW0_ALISL
LinkDB: B6ERW0_ALISL
Original site: B6ERW0_ALISL 
ID   B6ERW0_ALISL            Unreviewed;       437 AA.
AC   B6ERW0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Putative glucosyl transferase {ECO:0000313|EMBL:CAQ81444.1};
GN   OrderedLocusNames=VSAL_II0690 {ECO:0000313|EMBL:CAQ81444.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ81444.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ81444.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ81444.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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DR   EMBL; FM178380; CAQ81444.1; -; Genomic_DNA.
DR   RefSeq; WP_012551997.1; NC_011313.1.
DR   AlphaFoldDB; B6ERW0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; vsa:VSAL_II0690; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_023978_4_1_6; -.
DR   Proteomes; UP000001730; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06423; CESA_like; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR   PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:CAQ81444.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        22..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          152..373
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
SQ   SEQUENCE   437 AA;  50194 MW;  8E1CE0AB55D9E152 CRC64;
     MGEFQYVLHT ITGTLGAYWE LILTFIPIML VVEVPLMLFV FIGVLRWSWR DNHSVANVSP
     SISFVITCYR EGDGITQTID TLAEQIYPGE IEILIVVDGA KQNPKTYHAA LNGVYRHQSR
     ENRTLKVLPK WQRGGRVSTL NAGLAEAKND LVINVDGDTS FDNDVALRFA KSFSNPNVIA
     CGGALRVRNR DESFWTKMQA LEYMMSMQTS KTGMATWGLL NNISGAFGAF RRSIIKQVGG
     WDTHTGEDLD LTMRLKQYKG RYRNIELDFS PKAIGHTDVP ETFTGLMSQR LRWDGDLLFI
     YLRKHKQGLT PKLLGWGSFL YTLVYGVLQA VLLPLLITLF NFYLFLSFPN TVVFAVFSCL
     YVIYLFFIAL TFLVYLCLIS ERVKEDREML LWLIIYPFYA LFMRFVTAFS MVNEIVRRSH
     EESSMAPWWV LKRGKRF
//
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