ARNT_YERE8
ID ARNT_YERE8 Reviewed; 554 AA.
AC A1JPM4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE EC=2.4.2.43 {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=4-amino-4-deoxy-L-arabinose lipid A transferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase {ECO:0000255|HAMAP-Rule:MF_01165};
GN Name=arnT {ECO:0000255|HAMAP-Rule:MF_01165}; OrderedLocusNames=YE2188;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Catalyzes the transfer of the L-Ara4N moiety of the
CC glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The
CC modified arabinose is attached to lipid A and is required for
CC resistance to polymyxin and cationic antimicrobial peptides.
CC {ECO:0000255|HAMAP-Rule:MF_01165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-
CC undecaprenyl phosphate + lipid IVA = lipid IIA + di-trans,octa-cis-
CC undecaprenyl phosphate.; EC=2.4.2.43; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01165};
CC -!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
CC arabinose-lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01165}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01165}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01165}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000255|HAMAP-Rule:MF_01165}.
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DR EMBL; AM286415; CAL12258.1; -; Genomic_DNA.
DR RefSeq; WP_005169390.1; NC_008800.1.
DR RefSeq; YP_001006428.1; NC_008800.1.
DR AlphaFoldDB; A1JPM4; -.
DR SMR; A1JPM4; -.
DR STRING; 393305.YE2188; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; CAL12258; CAL12258; YE2188.
DR KEGG; yen:YE2188; -.
DR PATRIC; fig|393305.7.peg.2353; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0103015; F:4-amino-4-deoxy-L-arabinose transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR HAMAP; MF_01165; ArnT_transfer; 1.
DR InterPro; IPR022839; ArnT_tfrase.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR Pfam; PF02366; PMT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..554
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_1000065668"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ SEQUENCE 554 AA; 62340 MW; 575C24AD2DAC040E CRC64;
MKLLKGSGAA LLALFFALVY LLPINSRLLW QPDETRYAEI SREMLQRGDW VVPHLLGIRY
FEKPIAGYWF NNISQWIFGD TNFAVRFGSI FSTALSAVFV YWLATLLWRN RSTSFLAALI
YLSMLLVFSI GSYAVLDPMI SLWLTASMVC FYLTLRAETA KQKIGAYLLL GLACGMGFMT
KGFLALAVPV ISVLPIVIQQ KRVKELIIFG PIAIVGAVIL SLPWALAIAQ REPDFWHYFF
WVEHIQRFAE KDAQHKAPIW YYLPILCLGV LPWLGLLPAA LLKGWRERVA RPELFFLLSW
VLMPLIFFSV AKGKLPTYIL PCMAPLSLLM AAYATDCANK MHMRALKVNG AINLIFGFIC
ALAILVIGMG WVGHLVAYGP QEHQKVILAT IAFAGWGIVG FATMRNNARH WHWAAACPLL
FILLVGYLIP QQVIDSKQPQ NFIQNNFNEL SSSRYVATDS VGVAAGLAWE LKRSDILMFS
EKGELSYGLN YADSGDHYIS AQDFSDWLVH ARQKGDVSLV IQLSRNEKIP DSLPAADKVS
LMNRLALLWY KKTP
