ARNT_SALTI
ID ARNT_SALTI Reviewed; 547 AA.
AC Q8Z538; P81890; Q7CB86;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase;
DE EC=2.4.2.43;
DE AltName: Full=4-amino-4-deoxy-L-arabinose lipid A transferase;
DE AltName: Full=Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
DE AltName: Full=Melittin resistance protein PqaB;
DE AltName: Full=Polymyxin resistance protein PmrK;
DE AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase;
GN Name=arnT; Synonyms=pmrK, pqaB; OrderedLocusNames=STY2531, t0562;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=10075419; DOI=10.1099/13500872-145-2-367;
RA Baker S.J., Gunn J.S., Morona R.;
RT "The Salmonella typhi melittin resistance gene pqaB affects intracellular
RT growth in PMA-differentiated U937 cells, polymyxin B resistance and
RT lipopolysaccharide.";
RL Microbiology 145:367-378(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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 -!- 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;
CC -!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
CC arabinose-lipid A biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO68268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD07534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF071082; AAD20796.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO68268.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL513382; CAD07534.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_456844.1; NC_003198.1.
DR RefSeq; WP_024131156.1; NZ_LT905143.1.
DR AlphaFoldDB; Q8Z538; -.
DR SMR; Q8Z538; -.
DR STRING; 220341.16503526; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; AAO68268; AAO68268; t0562.
DR KEGG; stt:t0562; -.
DR KEGG; sty:STY2531; -.
DR PATRIC; fig|220341.7.peg.2562; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..547
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121511"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 159
FT /note="T -> M (in Ref. 1; AAD20796)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> A (in Ref. 1; AAD20796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 61631 MW; 3862538B57E48810 CRC64;
MKSIRYYLAF AAFIALYYVI PVNSRLLWQP DETRYAEISR EMLASGDWIV PHFLGLRYFE
KPIAGYWINS LGQWLFGATN FGVRAGAILT TLLAAALVAW LTFRLWRDKR TALLASVIFL
SLFAVYSIGT YAVLDPMIAL WLTAGMCCFW QGMQATTRTG KIGMFLLLGA TCGLGVLTKG
FLALAVPVVS VLPWVIVQKR WKDFLLYGWL AVLSCFVVVL PWAIAIARRE ADFWHYFFWV
EHIQRFAMSD AQHKAPFWYY LPVLLAGSLP WLGLLPGALK LGWRERNGAF YLLGWTIMPL
LFFSIAKGKL PTYVLSCFAP IAILMARFVL HNVKEGVAAL RVNGGINLVF GIIGIVAAFV
VSSWGPLKSP VWTHIETYKV FCVWGVFTVW AFVGWYSLCH SPKYLLPAFC PLGLALLFGF
SVPDRVMESK QPQFFVEMTQ APLASSRYIL ADSVGVAAGL AWSLKRDDIM LYGHAGELRY
GLSYPDVQNK FVKADDFNAW LNQHRQEGII TLVLSIDKDE DISALSLPPA DNVDYQGRLV
LIQYRPK
