ARNF_ECOLI
ID ARNF_ECOLI Reviewed; 128 AA.
AC P76474; Q2MAN0; Q47376;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF;
DE Short=L-Ara4N-phosphoundecaprenol flippase subunit ArnF;
DE AltName: Full=Undecaprenyl phosphate-aminoarabinose flippase subunit ArnF;
GN Name=arnF; Synonyms=pmrM, yfbJ; OrderedLocusNames=b2258, JW5373;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8626063; DOI=10.1016/0378-1119(95)00721-0;
RA Sharma V., Hudspeth M.E.S., Meganathan R.;
RT "Menaquinone (vitamin K2) biosynthesis: localization and characterization
RT of the menE gene from Escherichia coli.";
RL Gene 168:43-48(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP INDUCTION BY BASR.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15569938; DOI=10.1073/pnas.0406038101;
RA Winfield M.D., Groisman E.A.;
RT "Phenotypic differences between Salmonella and Escherichia coli resulting
RT from the disparate regulation of homologous genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17162-17167(2004).
RN [6]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
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: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol
CC (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the
CC periplasmic side of the inner membrane. {ECO:0000269|PubMed:17928292}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Heterodimer of ArnE and ArnF. {ECO:0000305|PubMed:17928292}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:15569938}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are polymyxin sensitive.
CC Lipid A is no longer modified with L-Ara4N even though the level of the
CC lipid-linked donor of the L-Ara4N moiety, alpha-L-Ara4N-
CC phosphoundecaprenol, is not reduced. However, the alpha-L-Ara4N-
CC phosphoundecaprenol is less concentrated on the periplasmic surface of
CC the inner membrane when compared to wild-type.
CC {ECO:0000269|PubMed:17928292}.
CC -!- SIMILARITY: Belongs to the ArnF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04894.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35031; AAB04894.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75318.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76676.1; -; Genomic_DNA.
DR PIR; H64996; H64996.
DR RefSeq; NP_416761.4; NC_000913.3.
DR RefSeq; WP_000523880.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P76474; -.
DR BioGRID; 4260501; 651.
DR DIP; DIP-48225N; -.
DR IntAct; P76474; 1.
DR STRING; 511145.b2258; -.
DR TCDB; 2.A.7.22.1; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; P76474; -.
DR PRIDE; P76474; -.
DR EnsemblBacteria; AAC75318; AAC75318; b2258.
DR EnsemblBacteria; BAE76676; BAE76676; BAE76676.
DR GeneID; 58461865; -.
DR GeneID; 945344; -.
DR KEGG; ecj:JW5373; -.
DR KEGG; eco:b2258; -.
DR PATRIC; fig|511145.12.peg.2351; -.
DR EchoBASE; EB3847; -.
DR eggNOG; COG2076; Bacteria.
DR HOGENOM; CLU_131462_1_0_6; -.
DR InParanoid; P76474; -.
DR OMA; AQLGMRW; -.
DR PhylomeDB; P76474; -.
DR BioCyc; EcoCyc:G7171-MON; -.
DR BioCyc; MetaCyc:G7171-MON; -.
DR UniPathway; UPA00030; -.
DR PRO; PR:P76474; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1901505; F:carbohydrate derivative transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1901264; P:carbohydrate derivative transport; IMP:EcoCyc.
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:0010041; P:response to iron(III) ion; IEP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR HAMAP; MF_00538; Flippase_ArnF; 1.
DR InterPro; IPR022832; Flippase_ArnF.
DR InterPro; IPR000390; Small_drug/metabolite_transptr.
DR PANTHER; PTHR30561; PTHR30561; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..128
FT /note="Probable 4-amino-4-deoxy-L-arabinose-
FT phosphoundecaprenol flippase subunit ArnF"
FT /id="PRO_0000218152"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..35
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 128 AA; 14085 MW; 1ACEEE17FDF6B446 CRC64;
MGLMWGLFSV IIASVAQLSL GFAASHLPPM THLWDFIAAL LAFGLDARIL LLGLLGYLLS
VFCWYKTLHK LALSKAYALL SMSYVLVWIA SMVLPGWEGT FSLKALLGVA CIMSGLMLIF
LPTTKQRY
