ARNT_ECOL6
ID ARNT_ECOL6 Reviewed; 550 AA.
AC Q8FFL9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=c2799;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81253.1; -; Genomic_DNA.
DR RefSeq; WP_000844038.1; NC_004431.1.
DR AlphaFoldDB; Q8FFL9; -.
DR SMR; Q8FFL9; -.
DR STRING; 199310.c2799; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; AAN81253; AAN81253; c2799.
DR KEGG; ecc:c2799; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR BioCyc; ECOL199310:C2799-MON; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000001410; 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..550
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121506"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 288..308
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 346..366
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ SEQUENCE 550 AA; 62552 MW; 204B12B17CA3665C CRC64;
MKSVRYLIGL FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE
KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLATVIYL
SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG
FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCVLTVL PWGLAIAQRE PDFWHYFFWV
EHIQRFALDD AQHRAPFWYY LPVVIAGSLP WLGLLPGALY AGWKNRKHSA TVYLLSWTIM
PLLFFSVAKG KLPTYILSCF APLAMLMAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT
FVVSPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWPFA ALCPLGLALL
VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE
LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PPADVIDRQE
RLVLIQYRPK
