ID A0A0D3VE10_9BACL Unreviewed; 765 AA.
AC A0A0D3VE10;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:AJS60350.1};
GN ORFNames=UB51_19990 {ECO:0000313|EMBL:AJS60350.1};
OS Paenibacillus sp. IHBB 10380.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS60350.1, ECO:0000313|Proteomes:UP000032320};
RN [1] {ECO:0000313|EMBL:AJS60350.1, ECO:0000313|Proteomes:UP000032320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS60350.1,
RC ECO:0000313|Proteomes:UP000032320};
RX PubMed=25908145;
RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT PacBio Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; CP010976; AJS60350.1; -; Genomic_DNA.
DR RefSeq; WP_044878792.1; NZ_CP010976.1.
DR AlphaFoldDB; A0A0D3VE10; -.
DR STRING; 1566358.UB51_19990; -.
DR KEGG; pih:UB51_19990; -.
DR PATRIC; fig|1566358.3.peg.4369; -.
DR HOGENOM; CLU_020629_0_0_9; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000032320; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd06427; CESA_like_2; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
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; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032320};
KW Transferase {ECO:0000313|EMBL:AJS60350.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..279
FT /note="Type II secretion system protein GspE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05157"
FT DOMAIN 463..655
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT COILED 18..73
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 765 AA; 88488 MW; 22B5FB1279C17F7A CRC64;
MKDRFRWQVR GLAFGQTKKL ILKERMELEQ LQQKLDEQRQ EQASGIHKLD FEIAGLNRRL
QETTVRIDQI QKDDELKKTA PTSGKGRMGE MLVSRGIITA AQLEHVILSQ KQYGGRLGDI
LVDMGFVTAE QMDRETAEAR PKERLGEMLV RSEYITQEQL DRALSFQAKS GGMLGDILLS
LQMLEPEELY RAIATQNQIG RIGEEIDLNV PFKLPEQWAQ DNGVIVVHQY LNRYLVAVED
PLPESRYAEL EALLGMPFEQ VLATKEELEQ LFSSIYGDEM LKHSTSKLKE QQPQNSASTT
FTFAQIMMFA IMGLSIIVGL IWNVWNTILV VNLLVQLFYF IMTVFKFWII YLGSRTDSQI
RFTPEEITAL DEKSLPIYTI LVPMYKEAGV VPHLIRNLEQ LDYPKSKLDV RLLIEEDDME
TKELLSSMNL PAYYTTLVVP DSLPKTKPKA CNYGLIRARG EYAVIYDAED QPDADQLKKV
MAAFNSLPEE YVCIQAKLNY FNSSQNLLTR WFTQEYSMWF ELLLPGIMKL DMPVPLGGTS
NHFKVSVLKD INAWDPYNVT EDADLGIRLY KSGYKTAIID SRTWEEANSQ VGNWIRQRSR
WIKGYMQTWL VHMRNPFKLI KEIGWKGFFG FQVMILATPL LPLLNPLFWL MIVLWFGWQA
EFIPKLFPGF LYYLAGAEFY IANFLFIFSN VAGVYWVIND LEEKGEKRFS FSLVKYGLST
PLYWVLMSIA AIKAAWQLVT KPFYWEKTVH GLADMHEEPE LREKL
//
