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Database: UniProt
Entry: K6U9Y4_9CLOT
LinkDB: K6U9Y4_9CLOT
Original site: K6U9Y4_9CLOT 
ID   K6U9Y4_9CLOT            Unreviewed;       407 AA.
AC   K6U9Y4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine synthase {ECO:0000256|ARBA:ARBA00017381, 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=A370_03186 {ECO:0000313|EMBL:EKQ54364.1};
OS   Clostridium sp. Maddingley MBC34-26.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ54364.1, ECO:0000313|Proteomes:UP000001325};
RN   [1] {ECO:0000313|EMBL:EKQ54364.1, ECO:0000313|Proteomes:UP000001325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX   PubMed=23405323;
RA   Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA   Midgley D.J., Hendry P.;
RT   "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT   Seam Gas Formation Water.";
RL   Genome Announc. 1:E00081-12(2013).
CC   -!- FUNCTION: N-acetylglucosaminyltransferase that catalyzes the
CC       polymerization of single monomer units of UDP-N-acetylglucosamine to
CC       produce the linear homomer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG,
CC       also referred to as PIA), a biofilm adhesin polysaccharide. Requires
CC       IcaD for full activity. {ECO:0000256|ARBA:ARBA00024738}.
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|ARBA:ARBA00006739, 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:EKQ54364.1}.
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DR   EMBL; ALXI01000102; EKQ54364.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6U9Y4; -.
DR   STRING; 1196322.A370_03186; -.
DR   PATRIC; fig|1196322.3.peg.3100; -.
DR   eggNOG; COG1215; Bacteria.
DR   Proteomes; UP000001325; 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; IPR001173; Glyco_trans_2-like.
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; PF00535; Glycos_transf_2; 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:UP000001325};
KW   Transferase {ECO:0000256|RuleBase:RU364028};
KW   Transmembrane {ECO:0000256|RuleBase:RU364028};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364028}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   TRANSMEM        301..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364028"
FT   DOMAIN          49..218
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   407 AA;  47615 MW;  5806732AB1068928 CRC64;
     MSKLIAYASS FVFWYPLIMS TVWIIGGVLF YYRREKKPGL PLNESPMVSI LVPCHNEENT
     IENTIKRLND LNYPNYEIIA INDGSKDKTE EILNNLSEEY EKLRVIQLKT NAGKANALYL
     GLVASKGEFL AGIDADAYLD SDALNYMIPH FITPNYGERV GAVTGNPRVR NRSSLLAKIQ
     LCESSSIISL IKRTQRLLGK VMTVSGVVVV FRKRALIDCG LWDRDLITED IGVTWKLQKR
     FWDIRYEPKA LCWMLVPETV VGLWKQRVRW AQGGLEVIMR HWNIFLSWKY RRLMPVYIEQ
     IFSIFWSITW FILFITMIIQ ITIGMQTFSS IFWQGQYLSF ICLIQFIIAM ALDKQYDEDL
     LKYYLWAIWY PTFFWYFSAL VILRAIPKAL FRNRKKFATW DSPDRGL
//
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