ARNC_ECOLI
ID ARNC_ECOLI Reviewed; 322 AA.
AC P77757; P78179; Q4U4N1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
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=pmrF, yfbF; OrderedLocusNames=b2254, JW2248;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15695810; DOI=10.1074/jbc.m414265200;
RA Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.;
RT "A formyltransferase required for polymyxin resistance in Escherichia coli
RT and the modification of lipid A with 4-amino-4-deoxy-L-arabinose:
RT identification and function of UDP-4-deoxy-4-formamido-L-arabinose.";
RL J. Biol. Chem. 280:14154-14167(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11706007; DOI=10.1074/jbc.m109377200;
RA Breazeale S.D., Ribeiro A.A., Raetz C.R.H.;
RT "Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-
RT resistant Escherichia coli. Origin of lipid A species modified with 4-
RT amino-4-deoxy-L-arabinose.";
RL J. Biol. Chem. 277:2886-2896(2002).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
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).
RN [7]
RP PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17928292; DOI=10.1074/jbc.m706172200;
RA Yan A., Guan Z., Raetz C.R.H.;
RT "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin
RT resistance in Escherichia coli.";
RL J. Biol. Chem. 282:36077-36089(2007).
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. {ECO:0000269|PubMed:11706007}.
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 Evidence={ECO:0000269|PubMed:15695810};
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. {ECO:0000269|PubMed:17928292}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:17928292}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by BasR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; DQ011863; AAY34350.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75314.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16077.1; -; Genomic_DNA.
DR PIR; D64996; D64996.
DR RefSeq; NP_416757.1; NC_000913.3.
DR RefSeq; WP_000461657.1; NZ_LN832404.1.
DR AlphaFoldDB; P77757; -.
DR SMR; P77757; -.
DR BioGRID; 4260496; 315.
DR IntAct; P77757; 3.
DR STRING; 511145.b2254; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.13; the putative vectorial glycosyl polymerization (vgp) family.
DR jPOST; P77757; -.
DR PaxDb; P77757; -.
DR PRIDE; P77757; -.
DR EnsemblBacteria; AAC75314; AAC75314; b2254.
DR EnsemblBacteria; BAA16077; BAA16077; BAA16077.
DR GeneID; 945275; -.
DR KEGG; ecj:JW2248; -.
DR KEGG; eco:b2254; -.
DR PATRIC; fig|1411691.4.peg.4483; -.
DR EchoBASE; EB3843; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_033536_0_0_6; -.
DR InParanoid; P77757; -.
DR OMA; DLVSGWK; -.
DR PhylomeDB; P77757; -.
DR BioCyc; EcoCyc:G7167-MON; -.
DR BioCyc; MetaCyc:G7167-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
DR PRO; PR:P77757; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; IDA:EcoCyc.
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 1: Evidence at protein 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..322
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000059195"
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..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 322 AA; 36339 MW; 4E293C24969C2679 CRC64;
MFEIHPVKKV SVVIPVYNEQ ESLPELIRRT TTACESLGKE YEILLIDDGS SDNSAHMLVE
ASQAENSHIV SILLNRNYGQ HSAIMAGFSH VTGDLIITLD ADLQNPPEEI PRLVAKADEG
YDVVGTVRQN RQDSWFRKTA SKMINRLIQR TTGKAMGDYG CMLRAYRRHI VDAMLHCHER
STFIPILANI FARRAIEIPV HHAEREFGES KYSFMRLINL MYDLVTCLTT TPLRMLSLLG
SIIAIGGFSI AVLLVILRLT FGPQWAAEGV FMLFAVLFTF IGAQFIGMGL LGEYIGRIYT
DVRARPRYFV QQVIRPSSKE NE
