ID B4EHA6_BURCJ Unreviewed; 423 AA.
AC B4EHA6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=BCAM1226 {ECO:0000313|EMBL:CAR55082.1};
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR55082.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR55082.1, ECO:0000313|Proteomes:UP000001035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC CF5610 {ECO:0000313|Proteomes:UP000001035};
RX PubMed=18931103; DOI=10.1128/JB.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM747721; CAR55082.1; -; Genomic_DNA.
DR RefSeq; WP_006488682.1; NC_011001.1.
DR AlphaFoldDB; B4EHA6; -.
DR SMR; B4EHA6; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 56561811; -.
DR KEGG; bcj:BCAM1226; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_023978_0_1_4; -.
DR BioCyc; BCEN216591:G1G1V-5229-MONOMER; -.
DR Proteomes; UP000001035; Chromosome 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364028};
KW Transmembrane {ECO:0000256|RuleBase:RU364028};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364028}.
FT TRANSMEM 15..36
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 343..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 376..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
SQ SEQUENCE 423 AA; 48061 MW; F484E7AEE1FA803D CRC64;
MTTHSLIQRL QDFVFYYPFF MSYLWMIGGV VHYFLLEEGR ELSTRTIASS GIPKVSIVVP
CFNEAANARS VIGHLNGMQY PNYDIIAVND GSKDRTGEIL NELAVEIPRL LVIHHARNEG
KAVGLTTAAA VSNAEYLLCI DGDALLAHDA IGWMLEHFLT DPGVGAVTGN PRIRTRTSLL
GRMQVGEFSS IVGLIKRTQQ VYGRIFTVSG VITMFRKTAL ADVGYWSSDM LTEDIDISWK
LQCRDWRVVY EPHALSWILM PETIKGLYRQ RLRWSKGGIQ VLLKYAGTLM RPTQMMMWPL
FAEYLIGIAW AYSMSFILLL ALIDVVYPLP PNWHVSVVPH WHGMLLVATC ILQLIIGSMI
DRRYDEKLLM YFLDTIWYPV AFWLISMITT VIALPAVVLR GRGKRAVWVS PDRGIQHEER
ADY
//