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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) (Polymyxin resistance protein PmrK) (Undecaprenyl phosphate-alpha-L-Ara4N transferase)

 ARNT_ECOLI              Reviewed;         550 AA.
P76473; Q2MAN2;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-MAR-2018, entry version 124.
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=Polymyxin resistance protein PmrK;
AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase;
Name=arnT; Synonyms=pmrK, yfbI; OrderedLocusNames=b2257, JW2251;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[3]
CATALYTIC ACTIVITY, AND FUNCTION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=11535604; DOI=10.1074/jbc.M106961200;
Trent M.S., Ribeiro A.A., Lin S., Cotter R.J., Raetz C.R.H.;
"An inner membrane enzyme in Salmonella and Escherichia coli that
transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on
polymyxin-resistant mutants and role of a novel lipid-linked donor.";
J. Biol. Chem. 276:43122-43131(2001).
[4]
SUBCELLULAR LOCATION.
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
-!- 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.
{ECO:0000269|PubMed:11535604}.
-!- CATALYTIC ACTIVITY: 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.
{ECO:0000269|PubMed:11535604}.
-!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
arabinose-lipid A biosynthesis.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
{ECO:0000269|PubMed:15919996}.
-!- INDUCTION: Induced by BasR. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
{ECO:0000305}.
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EMBL; U00096; AAC75317.1; -; Genomic_DNA.
EMBL; AP009048; BAE76674.1; -; Genomic_DNA.
PIR; G64996; G64996.
RefSeq; NP_416760.1; NC_000913.3.
RefSeq; WP_000844057.1; NZ_LN832404.1.
ProteinModelPortal; P76473; -.
BioGrid; 4260499; 153.
STRING; 316385.ECDH10B_2417; -.
CAZy; GT83; Glycosyltransferase Family 83.
TCDB; 9.B.142.2.9; the integral membrane glycosyltransferase family 39 (gt39) family.
PaxDb; P76473; -.
PRIDE; P76473; -.
EnsemblBacteria; AAC75317; AAC75317; b2257.
EnsemblBacteria; BAE76674; BAE76674; BAE76674.
GeneID; 947297; -.
KEGG; ecj:JW2251; -.
KEGG; eco:b2257; -.
PATRIC; fig|511145.12.peg.2349; -.
EchoBASE; EB3846; -.
EcoGene; EG14093; arnT.
eggNOG; ENOG4105SA9; Bacteria.
eggNOG; COG1807; LUCA.
HOGENOM; HOG000273002; -.
InParanoid; P76473; -.
KO; K07264; -.
OMA; TFWPGAP; -.
PhylomeDB; P76473; -.
BioCyc; EcoCyc:G7170-MONOMER; -.
BioCyc; MetaCyc:G7170-MONOMER; -.
BRENDA; 2.4.2.43; 2026.
UniPathway; UPA00037; -.
PRO; PR:P76473; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0016763; F:transferase activity, transferring pentosyl groups; IMP:EcoCyc.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:EcoCyc.
GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
GO; GO:0010041; P:response to iron(III) ion; IGI:EcoCyc.
HAMAP; MF_01165; ArnT_transfer; 1.
InterPro; IPR022839; ArnT_tfrase.
InterPro; IPR003342; Glyco_trans_39/83.
Pfam; PF02366; PMT; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 550 Undecaprenyl phosphate-alpha-4-amino-4-
deoxy-L-arabinose arabinosyl transferase.
/FTId=PRO_0000121504.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TRANSMEM 110 131 Helical. {ECO:0000255}.
TRANSMEM 137 154 Helical. {ECO:0000255}.
TRANSMEM 165 185 Helical. {ECO:0000255}.
TRANSMEM 204 224 Helical. {ECO:0000255}.
TRANSMEM 255 275 Helical. {ECO:0000255}.
TRANSMEM 288 308 Helical. {ECO:0000255}.
TRANSMEM 315 335 Helical. {ECO:0000255}.
TRANSMEM 346 366 Helical. {ECO:0000255}.
TRANSMEM 383 403 Helical. {ECO:0000255}.
TRANSMEM 406 426 Helical. {ECO:0000255}.
SEQUENCE 550 AA; 62543 MW; E57E0C3A0608D745 CRC64;
MKSVRYLIGL FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE
KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLATVIYL
SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG
FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCVLTVL PWGLAIAQRE PNFWHYFFWV
EHIQRFALDD AQHRAPFWYY VPVIIAGSLP WLGLLPGALY TGWKNRKHSA TVYLLSWTIM
PLLFFSVAKG KLPTYILSCF ASLAMLMAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT
FVVSPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWPFA ALCPLGLALL
VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE
LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PPADAIDRQE
RLVLIQYRPK


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