ID ARNT2_PSEPF Reviewed; 549 AA. AC Q3KCB9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 2 {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 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01165}; GN Name=arnT2 {ECO:0000255|HAMAP-Rule:MF_01165}; GN OrderedLocusNames=Pfl01_2845; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000094; ABA74586.1; -; Genomic_DNA. DR RefSeq; WP_011334257.1; NC_007492.2. DR AlphaFoldDB; Q3KCB9; -. DR SMR; Q3KCB9; -. DR CAZy; GT83; Glycosyltransferase Family 83. DR KEGG; pfo:Pfl01_2845; -. DR eggNOG; COG1807; Bacteria. DR HOGENOM; CLU_019200_2_1_6; -. DR UniPathway; UPA00037; -. DR Proteomes; UP000002704; Chromosome. 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 PANTHER; PTHR33908; MANNOSYLTRANSFERASE YKCB-RELATED; 1. DR PANTHER; PTHR33908:SF3; UNDECAPRENYL PHOSPHATE-ALPHA-4-AMINO-4-DEOXY-L-ARABINOSE ARABINOSYL TRANSFERASE; 1. 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..549 FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L- FT arabinose arabinosyl transferase 2" FT /id="PRO_0000380022" FT TRANSMEM 9..29 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 80..102 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 112..132 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 133..153 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 176..196 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 259..279 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 312..332 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 342..362 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 402..422 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" SQ SEQUENCE 549 AA; 61799 MW; BE48FCA63666F866 CRC64; MSKRWALPLL LGIFLLAYLL PLGSHGLWIP DETRYAQISQ EMLLSGNWVS PHFMNLRYFE KPAAGYWMIA IGQAVFGQNL FGVRFASALS TGLSVLLCFL IARRLWNEPR KSFVCALLYM SFVIVAGQAG YANLDPQFTF WVNLSLVALW FALDSRANGQ RLAGWAVLGL ACGMGFMTKG FLAWLLPVLI ALPWMLWQKR WKELLLYGPV AIAVAIIVSL PWALAVHGQE PDYWRFFFWH EHIRRFAGDD AQHDAPWWFY LPLLVAFSLP WVGMLPVAFK QAWQTRRETG IAFLGLWLLM PLLFFSLSNG KLPTYILPCL LPLALLLGHA LADRLRLEQG RALGLNGLLN LLLGLVTLIG LVYVQLKRPL YDHELHSLVL VFIALTGWII SNLLQAFRPL QCWAAPAVGS LLLIALLPAA LPRSVVANKM PDQFVLAHQK ELTATTHLLS NDLGAASALS WRVKRPQVAL YNTIGELKYG LAYPDGIQQR VDPDQVQQWM REARKTGSVG VVMRVKGQDE LDELDRLPKD GVRYEQGNLV IMILPQEAS //