ARNT_SALTY
ID ARNT_SALTY Reviewed; 547 AA.
AC O52327; Q7CQ57; Q8ZNF1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
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; OrderedLocusNames=STM2301;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=9570402; DOI=10.1046/j.1365-2958.1998.00757.x;
RA Gunn J.S., Lim K.B., Krueger J., Kim K., Guo L., Hackett M., Miller S.I.;
RT "PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A
RT modification and polymyxin resistance.";
RL Mol. Microbiol. 27:1171-1182(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 14028s / SGSG 2262;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA Woesten M.M.S.M., Groisman E.A.;
RT "Molecular characterization of the PmrA regulon.";
RL J. Biol. Chem. 274:27185-27190(1999).
RN [5]
RP REGULATION BY BASR AND BASS.
RX PubMed=11051552; DOI=10.1016/s0092-8674(00)00092-1;
RA Woesten M.M.S.M., Kox L.F.F., Chamnongpol S., Soncini F.C., Groisman E.A.;
RT "A signal transduction system that responds to extracellular iron.";
RL Cell 103:113-125(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16226890; DOI=10.1016/j.pep.2005.08.028;
RA Bretscher L.E., Morrell M.T., Funk A.L., Klug C.S.;
RT "Purification and characterization of the L-Ara4N transferase protein ArnT
RT from Salmonella typhimurium.";
RL Protein Expr. Purif. 46:33-39(2006).
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, ECO:0000269|PubMed:16226890}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {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:16226890}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16226890}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:10480935}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL21202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL34393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF036677; AAC04774.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY057444; AAL34393.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL21202.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_461243.1; NC_003197.2.
DR AlphaFoldDB; O52327; -.
DR SMR; O52327; -.
DR STRING; 99287.STM2301; -.
DR ChEMBL; CHEMBL1075254; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR PaxDb; O52327; -.
DR EnsemblBacteria; AAL21202; AAL21202; STM2301.
DR GeneID; 1253823; -.
DR KEGG; stm:STM2301; -.
DR PATRIC; fig|99287.12.peg.2436; -.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR PhylomeDB; O52327; -.
DR BRENDA; 2.4.2.43; 5542.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR GO; GO:0010041; P:response to iron(III) ion; IBA:GO_Central.
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..547
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121512"
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 162..184
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"
SQ SEQUENCE 547 AA; 61690 MW; 0FB8B2462510EE4E CRC64;
MKSIRYYLAF AAFIALYYVI PVNSRLLWQP DETRYAEISR EMLASGDWIV PHFLGLRYFE
KPIAGYWINS LGQWLFGATN FGVRAGAILT TLLAAALVAW LTFRLWRDKR TALLASVIFL
SLFAVYSIGT YAVLDPMIAL WLTAGMCCFW QGMQATTRMG KIGMFLLLGA TCGLGVLTKG
FLALAVPVVS VLPWVIVQKR WKDFLLYGWL AVLSCFVVVL PWAIAIARRE ADFWHYFFWV
EHIQRFAMSD AQHKAPFWYY LPVLLAGSLP WLGLLPGALK LGWRERNGAF YLLGWTIMPL
LFFSIAKGKL PTYVLSCFAP IAILMARFVL HNVKEGVAAL RVNGGINLVF GLVGIVAAFV
VSSWGPLKSP VWTHIETYKV FCVWGVFTVW AFVGWYSLCH SQKYLLPAFC PLGLALLFGF
SIPDRVMESK QPQFFVEMTQ APLASSRYIL ADNVGVAAGL AWSLKRDDIM LYGHAGELRY
GLSYPDVQDK FVKADDFNAW LNQHRQEGII TLVLSIAKDE DISALSLPPA DNIDYQGRLV
LIQYRPK
