ARNC_SALTY
ID ARNC_SALTY Reviewed; 327 AA.
AC O52324; Q8ZNF2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase;
DE EC=2.4.2.53;
DE AltName: Full=Polymyxin resistance protein PmrF;
DE AltName: Full=Undecaprenyl-phosphate Ara4FN transferase;
DE Short=Ara4FN transferase;
GN Name=arnC; Synonyms=pbgP2, pmrF; OrderedLocusNames=STM2298;
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], AND FUNCTION.
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 [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 [3]
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 [4]
RP INDUCTION.
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).
CC -!- FUNCTION: Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose
CC from UDP to undecaprenyl phosphate. The modified arabinose is attached
CC to lipid A and is required for resistance to polymyxin and cationic
CC antimicrobial peptides. Plays an important role in pathogenesis by
CC providing resistance to antimicrobial peptides within macrophages or at
CC other anatomic sites encountered during infection.
CC {ECO:0000269|PubMed:9570402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-4-deoxy-4-
CC formamido-beta-L-arabinose = 4-deoxy-4-formamido-alpha-L-
CC arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP;
CC Xref=Rhea:RHEA:27722, ChEBI:CHEBI:58223, ChEBI:CHEBI:58709,
CC ChEBI:CHEBI:58909, ChEBI:CHEBI:60392; EC=2.4.2.53;
CC -!- PATHWAY: Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose
CC and undecaprenyl phosphate: step 1/2.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:10480935,
CC ECO:0000269|PubMed:11051552}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {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; AF036677; AAC04771.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21199.1; -; Genomic_DNA.
DR RefSeq; NP_461240.1; NC_003197.2.
DR RefSeq; WP_000458893.1; NC_003197.2.
DR AlphaFoldDB; O52324; -.
DR SMR; O52324; -.
DR STRING; 99287.STM2298; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; O52324; -.
DR EnsemblBacteria; AAL21199; AAL21199; STM2298.
DR GeneID; 1253820; -.
DR KEGG; stm:STM2298; -.
DR PATRIC; fig|99287.12.peg.2433; -.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OMA; DLVSGWK; -.
DR PhylomeDB; O52324; -.
DR BioCyc; SENT99287:STM2298-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:UniProtKB-UniRule.
DR GO; GO:0099621; F:undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036108; P:4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01164; ArnC_transfer; 1.
DR InterPro; IPR022857; ArnC_tfrase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000059203"
FT TOPO_DOM 1..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..269
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 327 AA; 36516 MW; CE695B419348126F CRC64;
MFDAAPIKKV SVVIPVYNEQ ESLPELIRRT TTACESLGKA WEILLIDDGS SDSSAELMVK
ASQEADSHII SILLNRNYGQ HAAIMAGFSH VSGDLIITLD ADLQNPPEEI PRLVAKADEG
FDVVGTVRQN RQDSLFRKSA SKIINLLIQR TTGKAMGDYG CMLRAYRRPI IDTMLRCHER
STFIPILANI FARRATEIPV HHAEREFGDS KYSFMRLINL MYDLVTCLTT TPLRLLSLLG
SVIAIGGFSL SVLLIVLRLA LGPQWAAEGV FMLFAVLFTF IGAQFIGMGL LGEYIGRIYN
DVRARPRYFV QQVIYPESTP FTEESHQ
