ARNT_YERPS
ID ARNT_YERPS Reviewed; 554 AA.
AC Q66A06; Q93PD6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=YPTB2326;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=32777 / IP2777 / Serotype O1:b;
RX PubMed=15583148; DOI=10.1099/mic.0.27426-0;
RA Marceau M.B., Sebbane F., Ewann F., Collyn F., Lindner B., Campos M.A.,
RA Bengoechea J.-A., Simonet M.;
RT "The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is
RT upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and
RT is not required for virulence.";
RL Microbiology 150:3947-3957(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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 (By
CC similarity). {ECO:0000250}.
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 -!- INDUCTION: Activated by low magnesium concentrations, via the two-
CC component regulatory system PhoP/PhoQ. {ECO:0000269|PubMed:15583148}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
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DR EMBL; AF336802; AAK69644.1; -; Genomic_DNA.
DR EMBL; BX936398; CAH21564.1; -; Genomic_DNA.
DR RefSeq; WP_002211821.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66A06; -.
DR SMR; Q66A06; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; CAH21564; CAH21564; YPTB2326.
DR GeneID; 66841240; -.
DR KEGG; ypo:BZ17_128; -.
DR KEGG; yps:YPTB2326; -.
DR PATRIC; fig|273123.14.peg.137; -.
DR OMA; TFWPGAP; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000001011; 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 2: Evidence at transcript level;
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..554
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121516"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 514
FT /note="E -> K (in Ref. 1; AAK69644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62289 MW; 11BFF54C66FBDB48 CRC64;
MKLLKDSGAA LLALFFVLVY LLPVNSRLLW QPDETRYAEI SREMLQRGDW VVPYFMDIRY
FEKPVAGYWF NNISQWIFGD SNFAVRFGSI FSTALSAVLV YWLATLLWRN RSTSVLATLI
YLSFLLVFGI GTYAVLDPMI SLWLTAAMVS FYLTLKAENW QQKVGAYALL GVACGMGFMT
KGFLALAVPV IAVLPIVIQQ KRIKDLVVFG PIAIVCAVLL SLPWALAIAQ REPDFWNYFF
WVEHIQRFAE ASAQHKSPIW YYLPILCIGV LPWLGLLPGA LFKGWRERAT KPELFFLLSW
VVMPLLFFSV AKGKLPTYIL PCMAPLSLLM AAYATDCANN IRMRALKING VINLLFGVAC
ALVIVVIGLG LVKDIVAYGP QENQKVWLGV LAFAGWGVTG FITLRNNARN WRWAAACPLL
FILLVGYLIP QQVVDSKQPQ NFIKNNFSEL SSSRYVLTDS VGVAAGLAWE LKRSDILMFS
EKGELTYGLA YPDSQDNYIS NDDFPTWLAQ ARKEGDVSLV VQLAKNEALP AHLPPADKVN
LMNRLALLWY QKTP
