ARNT_ECOLI
ID ARNT_ECOLI Reviewed; 550 AA.
AC P76473; Q2MAN2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
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=Polymyxin resistance protein PmrK;
DE AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase;
GN Name=arnT; Synonyms=pmrK, yfbI; OrderedLocusNames=b2257, JW2251;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11535604; DOI=10.1074/jbc.m106961200;
RA Trent M.S., Ribeiro A.A., Lin S., Cotter R.J., Raetz C.R.H.;
RT "An inner membrane enzyme in Salmonella and Escherichia coli that transfers
RT 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant
RT mutants and role of a novel lipid-linked donor.";
RL J. Biol. Chem. 276:43122-43131(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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:0000269|PubMed:11535604}.
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 Evidence={ECO:0000269|PubMed:11535604};
CC -!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
CC arabinose-lipid A biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75317.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76674.1; -; Genomic_DNA.
DR PIR; G64996; G64996.
DR RefSeq; NP_416760.1; NC_000913.3.
DR RefSeq; WP_000844057.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P76473; -.
DR SMR; P76473; -.
DR BioGRID; 4260499; 153.
DR STRING; 511145.b2257; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR TCDB; 9.B.142.2.9; the integral membrane glycosyltransferase family 39 (gt39) family.
DR jPOST; P76473; -.
DR PaxDb; P76473; -.
DR PRIDE; P76473; -.
DR EnsemblBacteria; AAC75317; AAC75317; b2257.
DR EnsemblBacteria; BAE76674; BAE76674; BAE76674.
DR GeneID; 947297; -.
DR KEGG; ecj:JW2251; -.
DR KEGG; eco:b2257; -.
DR PATRIC; fig|511145.12.peg.2349; -.
DR EchoBASE; EB3846; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR InParanoid; P76473; -.
DR OMA; TFWPGAP; -.
DR PhylomeDB; P76473; -.
DR BioCyc; EcoCyc:G7170-MON; -.
DR BioCyc; MetaCyc:G7170-MON; -.
DR BRENDA; 2.4.2.43; 2026.
DR UniPathway; UPA00037; -.
DR PRO; PR:P76473; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0016763; F:pentosyltransferase activity; IMP:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR GO; GO:0010041; P:response to iron(III) ion; IEP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..550
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121504"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
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 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ 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
