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Database: UniProt
Entry: A0A0J6NL65_9NEIS
LinkDB: A0A0J6NL65_9NEIS
Original site: A0A0J6NL65_9NEIS 
ID   A0A0J6NL65_9NEIS        Unreviewed;       413 AA.
AC   A0A0J6NL65;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine synthase {ECO:0000256|RuleBase:RU364028};
DE            Short=Poly-beta-1,6-GlcNAc synthase {ECO:0000256|RuleBase:RU364028};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU364028};
GN   ORFNames=VK98_13665 {ECO:0000313|EMBL:KMN81422.1};
OS   Chromobacterium sp. LK11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN81422.1, ECO:0000313|Proteomes:UP000036114};
RN   [1] {ECO:0000313|EMBL:KMN81422.1, ECO:0000313|Proteomes:UP000036114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LK11 {ECO:0000313|EMBL:KMN81422.1,
RC   ECO:0000313|Proteomes:UP000036114};
RA   Chan X.Y.;
RT   "Draft genome of Chromobacterium aquaticum LK11.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364028};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU364028}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|RuleBase:RU364028}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU364028}.
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:KMN81422.1}.
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DR   EMBL; LDUR01000020; KMN81422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6NL65; -.
DR   STRING; 1628212.VK98_13665; -.
DR   PATRIC; fig|1628212.3.peg.1824; -.
DR   OrthoDB; 276604at2; -.
DR   Proteomes; UP000036114; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:InterPro.
DR   GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
DR   CDD; cd06423; CESA_like; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR023853; PGA_PgaC/IcaA.
DR   NCBIfam; TIGR03937; PgaC_IcaA; 1.
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; PF13641; Glyco_tranf_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU364028};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364028};
KW   Membrane {ECO:0000256|RuleBase:RU364028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036114};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364028};
KW   Transmembrane {ECO:0000256|RuleBase:RU364028};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364028}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   TRANSMEM        299..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   TRANSMEM        376..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
SQ   SEQUENCE   413 AA;  47743 MW;  3B7C9EA0524CB01C CRC64;
     MALILLLAYA FFYPLFMAYL WMVGAVHYYL HYERKDPPLN QPPTLDYPPL SVVVPCYNEE
     DNVRETLAYA LALDYPDFEV IAVNDGSRDA TGAILDELAA AHPRLRVVHQ ATNQGKAVGL
     NTALALARHE YLLCIDGDAL LDPYAGKWLM RHFLTSPRVG AVTGNPRIRN RTTLLGRLQV
     GEFTAIIGLI KRAQRTYGRL FTVSGVITAF RKTAVYQAGY WSEDMLTEDI DISWKLQLKH
     WNVRFEPRAL VWILMPETLR GLWKQRLRWA KGGTQALMRN AWVLRTWRHR HMWPVYSEYF
     LSVVWSYTMA GIIVYWLLSL VLGDWLPQVG TPLIPRWHGM VLGGTCMLQF MISKMMDSQY
     DAKLGKNYYW MVWYPLVYWL LNVCTTIVAF PQAVFRKKGK RARWVSPDRG VRA
//
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