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Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase (EC 2.4.2.43) (4-amino-4-deoxy-L-arabinose lipid A transferase) (Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase) (Melittin resistance protein PqaB) (Polymyxin resistance protein PmrK) (Undecaprenyl phosphate-alpha-L-Ara4N transferase)

 ARNT_SALTI              Reviewed;         547 AA.
Q8Z538; P81890; Q7CB86;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
05-DEC-2018, entry version 103.
RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase;
EC=2.4.2.43;
AltName: Full=4-amino-4-deoxy-L-arabinose lipid A transferase;
AltName: Full=Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
AltName: Full=Melittin resistance protein PqaB;
AltName: Full=Polymyxin resistance protein PmrK;
AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase;
Name=arnT; Synonyms=pmrK, pqaB; OrderedLocusNames=STY2531, t0562;
Salmonella typhi.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=90370;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
PubMed=10075419; DOI=10.1099/13500872-145-2-367;
Baker S.J., Gunn J.S., Morona R.;
"The Salmonella typhi melittin resistance gene pqaB affects
intracellular growth in PMA-differentiated U937 cells, polymyxin B
resistance and lipopolysaccharide.";
Microbiology 145:367-378(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CT18;
PubMed=11677608; DOI=10.1038/35101607;
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
Whitehead S., Barrell B.G.;
"Complete genome sequence of a multiple drug resistant Salmonella
enterica serovar Typhi CT18.";
Nature 413:848-852(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
and CT18.";
J. Bacteriol. 185:2330-2337(2003).
-!- FUNCTION: Catalyzes the transfer of the L-Ara4N moiety of the
glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The
modified arabinose is attached to lipid A and is required for
resistance to polymyxin and cationic antimicrobial peptides.
-!- CATALYTIC ACTIVITY:
Reaction=4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-
cis-undecaprenyl phosphate + lipid IV(A) = lipid II(A) + di-
trans,octa-cis-undecaprenyl phosphate.; EC=2.4.2.43;
-!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
arabinose-lipid A biosynthesis.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD20796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAO68268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAD07534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF071082; AAD20796.1; ALT_INIT; Genomic_DNA.
EMBL; AE014613; AAO68268.1; ALT_INIT; Genomic_DNA.
EMBL; AL513382; CAD07534.1; ALT_INIT; Genomic_DNA.
RefSeq; NP_456844.1; NC_003198.1.
RefSeq; WP_024131156.1; NZ_LT905143.1.
STRING; 220341.STY2531; -.
CAZy; GT83; Glycosyltransferase Family 83.
EnsemblBacteria; AAO68268; AAO68268; t0562.
EnsemblBacteria; CAD07534; CAD07534; CAD07534.
GeneID; 1248857; -.
KEGG; stt:t0562; -.
KEGG; sty:STY2531; -.
PATRIC; fig|220341.7.peg.2562; -.
eggNOG; ENOG4105SA9; Bacteria.
eggNOG; COG1807; LUCA.
HOGENOM; HOG000273002; -.
KO; K07264; -.
UniPathway; UPA00037; -.
Proteomes; UP000000541; Chromosome.
Proteomes; UP000002670; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0103015; F:4-amino-4-deoxy-L-arabinose transferase activity; IEA:UniProtKB-EC.
GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
HAMAP; MF_01165; ArnT_transfer; 1.
InterPro; IPR022839; ArnT_tfrase.
InterPro; IPR003342; Glyco_trans_39/83.
Pfam; PF02366; PMT; 1.
3: Inferred from homology;
Cell inner membrane; Cell membrane; Complete proteome;
Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 547 Undecaprenyl phosphate-alpha-4-amino-4-
deoxy-L-arabinose arabinosyl transferase.
/FTId=PRO_0000121511.
TRANSMEM 8 28 Helical. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TRANSMEM 113 133 Helical. {ECO:0000255}.
TRANSMEM 136 156 Helical. {ECO:0000255}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TRANSMEM 204 224 Helical. {ECO:0000255}.
TRANSMEM 255 275 Helical. {ECO:0000255}.
TRANSMEM 288 308 Helical. {ECO:0000255}.
TRANSMEM 310 330 Helical. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TRANSMEM 380 400 Helical. {ECO:0000255}.
TRANSMEM 404 424 Helical. {ECO:0000255}.
CONFLICT 159 159 T -> M (in Ref. 1; AAD20796).
{ECO:0000305}.
CONFLICT 349 349 V -> A (in Ref. 1; AAD20796).
{ECO:0000305}.
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


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