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ARNT_ENT38
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   03-AUG-2022, entry version 89.
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=Ent638_2075;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   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}.
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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   CAZy; GT83; Glycosyltransferase Family 83.
DR   EnsemblBacteria; ABP60751; ABP60751; Ent638_2075.
DR   KEGG; ent:Ent638_2075; -.
DR   eggNOG; COG1807; Bacteria.
DR   HOGENOM; CLU_019200_2_1_6; -.
DR   OMA; TFWPGAP; -.
DR   OrthoDB; 854536at2; -.
DR   UniPathway; UPA00037; -.
DR   Proteomes; UP000000230; 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..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
 
 
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