ID Q5QFG3_ACTPL Unreviewed; 411 AA.
AC Q5QFG3;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 Name=aagC {ECO:0000313|EMBL:AAT46092.1};
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715 {ECO:0000313|EMBL:AAT46092.1};
RN [1] {ECO:0000313|EMBL:AAT46092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IA1 {ECO:0000313|EMBL:AAT46092.1};
RX PubMed=15576769; DOI=10.1128/JB.186.24.8213-8220.2004;
RA Kaplan J.B., Velliyagounder K., Ragunath C., Rohde H., Mack D.,
RA Knobloch J.K., Ramasubbu N.;
RT "Genes involved in the synthesis and degradation of matrix polysaccharide
RT in Actinobacillus actinomycetemcomitans and Actinobacillus pleuropneumoniae
RT biofilms.";
RL J. Bacteriol. 186:8213-8220(2004).
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}.
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DR EMBL; AY618480; AAT46092.1; -; Genomic_DNA.
DR RefSeq; WP_005599666.1; NZ_UIFY01000002.1.
DR AlphaFoldDB; Q5QFG3; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR OrthoDB; 276604at2; -.
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 Transferase {ECO:0000256|RuleBase:RU364028};
KW Transmembrane {ECO:0000256|RuleBase:RU364028};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364028}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT TRANSMEM 376..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364028"
FT DOMAIN 53..216
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 411 AA; 47341 MW; 0E14A38479A12DB3 CRC64;
MILEIFSLFV FAYPAVMAFY WAFAGLTYFL FKEKLKVPPN FDQMKHEEVP LVSLMVPCYN
ESDNLDEAIP HLLNLKYPNY ELIFINDGSK DHTGEIIDKW AKRDKRIVAL HQANSGKASA
LNNGLRIARG KYVGCIDGDA VLDYKALDYM VQALESNPRY GAVTGNPRVR NRSTILGRLQ
VSEFSSIIGL IKRAQCLMGT IFTVSGVCCL FRKDIMFEIG GWSTNMITED IDVSWKIQTS
GYDIFYEPRA LCWVLMPETI NGLFKQRLRW AQGGAETMMK YFPQIWRLKN RRLWPMFIEY
IVTAIWASLL LVSILLSIYN LIFDNQIGLL DWAELKPSIA ILFIAFFTQL SISLYIDNRY
EKGVVKYAFS CIWYPWLYWS LNTITLLCGI PKAIFRNKTK LAVWTSPDRG V
//
