ID ARNT_ENT38 Reviewed; 553 AA. AC A4WAM1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 105. 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}; GN OrderedLocusNames=Ent638_2075; OS Enterobacter sp. (strain 638). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638; RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943; RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., RA Vangronsveld J., Newman L., Monchy S.; RT "Genome sequence of the plant growth promoting endophytic bacterium RT Enterobacter sp. 638."; RL PLoS Genet. 6:E1000943-E1000943(2010). 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; CP000653; ABP60751.1; -; Genomic_DNA. DR RefSeq; WP_012017466.1; NC_009436.1. DR AlphaFoldDB; A4WAM1; -. DR SMR; A4WAM1; -. DR STRING; 399742.Ent638_2075; -. DR KEGG; ent:Ent638_2075; -. DR eggNOG; COG1807; Bacteria. DR HOGENOM; CLU_019200_2_1_6; -. DR OrthoDB; 9775035at2; -. DR UniPathway; UPA00037; -. DR Proteomes; UP000000230; 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:TreeGrafter. DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro. DR GO; GO:0010041; P:response to iron(III) ion; IEA:TreeGrafter. DR HAMAP; MF_01165; ArnT_transfer; 1. DR InterPro; IPR022839; ArnT. DR InterPro; IPR003342; ArnT-like_N. DR InterPro; IPR061924; ArnT_C_gammaproteobact. DR InterPro; IPR050297; LipidA_mod_glycosyltrf_83. DR NCBIfam; NF009784; PRK13279.1; 1. 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; PF30401; ArnT_C_2; 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; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..553 FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L- FT arabinose arabinosyl transferase" FT /id="PRO_1000065665" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 111..131 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 132..152 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 255..275 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 317..337 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 350..370 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 380..400 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" FT TRANSMEM 407..427 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165" SQ SEQUENCE 553 AA; 61876 MW; 7DE7980845DCE26C CRC64; MKSAQYSLVL LLGFTLLYLL PLEFRALWQP DETRYAEISR EMLSAGNWIV PHFLDVRYFE KPVAGYWINN LSQMIFGHNN FSVRFGAVFS TTLSALMVAW LAFRLWRDKT VAVLSGVIFL TCLLVYGVGT YAVLDPMITL WLVAAMCSFW LGANAQTRAG KAGGYILLGL ACGMGVMTKG FLALAVPVLG VLPWVIAQKR WKEVLLFGPL AIISATLITL PWALAIAKAE PTFWHYFFWV EHIQRFAEND AQHKAPFWYY IPFLIAGCLP WVALLPGALK RSWNERHIES GTLYLLGWVV MPLLFFSIAK GKLPTYILPC FAPLAILLAR HATQLVATPR TLKVNGWINT VFGAVCALIV LLVLAPWGIA KHPIYASHEV LKVIQASIAF LVWALVGYLT TRNNARLWQW AALCPLGIAL LVGGMIPDKV VYSKHPQAFV DLVRPELESS RYILADSVGV GAGIAWEMKR SDITLYAKPG ELDYGLTTFA DAKDNFVSRD DFASWLALHR KEGNVSLVKL LSKDSVLEDS DVPAPDKVYH KGRFLLFFYE KTP //