ARNT1_PSEPF
ID ARNT1_PSEPF Reviewed; 569 AA.
AC Q3KCC9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 1 {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 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01165};
GN Name=arnT1 {ECO:0000255|HAMAP-Rule:MF_01165}; OrderedLocusNames=Pfl01_2835;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; 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}.
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DR EMBL; CP000094; ABA74576.1; -; Genomic_DNA.
DR RefSeq; WP_011334247.1; NC_007492.2.
DR AlphaFoldDB; Q3KCC9; -.
DR SMR; Q3KCC9; -.
DR STRING; 205922.Pfl01_2835; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; ABA74576; ABA74576; Pfl01_2835.
DR KEGG; pfo:Pfl01_2835; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; DFWRFFF; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000002704; 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..569
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase 1"
FT /id="PRO_0000380021"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ SEQUENCE 569 AA; 64200 MW; D39B98D70216EC38 CRC64;
MTSENNPLRH TALFPSTTAV ERWAIPGLIL AFVMFYLLPL MSHGLWIPDE TRYGQISQEM
LLSGNWVAPH FMGIRYFEKP IAGYWMIAIG QAIFGDNLFG VRIASALSTG VSVWLTYLLA
RRLWNNPRIN AASALLYMSF GLIAGQAGYA NLDPQFTLWV NLSMVAVWFA IDNRTPRARL
GGWALLGVAC GMGLMTKGFL ALLLPVLIAL PYMLWQRRFG ELVRYGLVAV VVCALVSLPW
VLAVHYREPD FWRFFFWHEH IRRFAAGDDA QHARPWWFYL PLLFASTLPW ALLLPSTLLR
MWREKREAKM AYLALWFLLP LAFFSLSSGK LPTYIMPCLL PVALLMGQTV VKWLDQRSGR
FLRLNGVFNT VLASVALVAL LYLQATKEIY ENTEMFSLSL AYIVVVGWII ANALQVLRPL
TLWAMPALGI GLLVALLPAA MPAQIVNSKM PDQFIAEHQR ELSETASLLS NDLGAASALA
WRLKRPQVDL FNTIGELKYG LEDPAMEARK VTMDGVGQWM TEARKKGAVG VVLRVNSTQE
EQEVELLPVD GKHYRRGNLH IFIFAQKQP
