ID A0A1I3N1G9_9RHOB Unreviewed; 655 AA.
AC A0A1I3N1G9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SFJ03069.1};
GN ORFNames=SAMN05216258_11287 {ECO:0000313|EMBL:SFJ03069.1};
OS Albimonas pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFJ03069.1, ECO:0000313|Proteomes:UP000199377};
RN [1] {ECO:0000313|EMBL:SFJ03069.1, ECO:0000313|Proteomes:UP000199377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFJ03069.1,
RC ECO:0000313|Proteomes:UP000199377};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; FOQH01000012; SFJ03069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3N1G9; -.
DR STRING; 1114924.SAMN05216258_11287; -.
DR OrthoDB; 7431422at2; -.
DR Proteomes; UP000199377; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
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 Pfam; PF05157; MshEN; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199377};
KW Transferase {ECO:0000313|EMBL:SFJ03069.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 528..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..154
FT /note="Type II secretion system protein GspE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05157"
FT DOMAIN 358..552
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 70165 MW; E5C5B2D0080A6866 CRC64;
MSSPSSPPAP RRAGREVSPL APRPGPRRPP SERLGALLVR DGAASELSIA VALRRQRRSG
APLGEILLAH GLVSPEAVAR AVARQMGIEV ADLAAHPPDP ALLAATPLQA MATWRAAPWR
RDEGDPRRVT LATPDPARLL RDPEAVRRAF DLPRDTRLRA AVCTGAGLDA ALMAVPGERR
AARAAGRAPR SLSAQGLSGP RARIALAAAL LAIPAAAVVE PGAVLALVFL AALAFNAANM
AVRVAALFMA PERPAPAAPP PPEPTAATPC VTLLIALYKE PQAAPGLIAA LRRLDYPAER
LEAILAVEHD DPETVAAIHA ADPPPWLRVI AAPPGGPRTK PRALNHALDF ARGTIVGVYD
AEDRPDPDQI RKAVEGFARS PPRVACLQAR LRISNGREGW LSRCFAMEYA AWFHLVLPAL
VRMGAPVPLA GTSLFIRRRV LERVGGWDAW NVTEDADLGV RLARAGYLTR MFDSDTGEEA
VTRPGAWLRQ RSRWQKGYLQ TWQIHMRDPW RLWRELGWRG FLGMQVHFVG AGAAFLSQPL
FWTALFAWPL LAGGSPLLDR PGWTVLLLLG FMHAGQGVLL ASVLVGLRRA GWRISLAQAL
VLPFYWPLAT LAAFKALKES VTAPAYWDKT GHGAGPAVEG AATIRRSGRA AGAGG
//