ARAF_ECOLI
ID ARAF_ECOLI Reviewed; 329 AA.
AC P02924;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=L-arabinose-binding periplasmic protein;
DE Short=ABP;
DE Flags: Precursor;
GN Name=araF; OrderedLocusNames=b1901, JW1889;
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=BEK 180;
RX PubMed=2445996; DOI=10.1016/0022-2836(87)90607-3;
RA Scripture J.B., Voelker C., Miller S., O'Donnell R.T., Polgar L., Rade J.,
RA Horazdovsky B.F., Hogg R.W.;
RT "High-affinity L-arabinose transport operon. Nucleotide sequence and
RT analysis of gene products.";
RL J. Mol. Biol. 197:37-46(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=6885805; DOI=10.1016/s0021-9258(17)44353-5;
RA Scripture J.B., Hogg R.W.;
RT "The nucleotide sequences defining the signal peptides of the galactose-
RT binding protein and the arabinose-binding protein.";
RL J. Biol. Chem. 258:10853-10855(1983).
RN [6]
RP PROTEIN SEQUENCE OF 24-329.
RC STRAIN=B/R;
RX PubMed=326784; DOI=10.1016/s0021-9258(17)40167-0;
RA Hogg R.W., Hermodson M.A.;
RT "Amino acid sequence of the L-arabinose-binding protein from Escherichia
RT coli B/r.";
RL J. Biol. Chem. 252:5135-5141(1977).
RN [7]
RP PROTEIN SEQUENCE OF 24-35.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP INDUCTION.
RX PubMed=2231717; DOI=10.1016/s0022-2836(05)80163-9;
RA Hendrickson W., Stoner C., Schleif R.;
RT "Characterization of the Escherichia coli araFGH and araJ promoters.";
RL J. Mol. Biol. 215:497-510(1990).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-329.
RX PubMed=7031057; DOI=10.1016/s0021-9258(18)43029-3;
RA Newcomer M.E., Gilliland G.L., Quiocho F.A.;
RT "L-arabinose-binding protein-sugar complex at 2.4-A resolution.
RT Stereochemistry and evidence for a structural change.";
RL J. Biol. Chem. 256:13213-13217(1981).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-329.
RX PubMed=326785; DOI=10.1016/s0021-9258(17)40168-2;
RA Quiocho F.A., Gilliland G.L., Phillips G.N. Jr.;
RT "The 2.8-A resolution structure of the L-arabinose-binding protein from
RT Escherichia coli. Polypeptide chain folding, domain similarity, and
RT probable location of sugar-binding site.";
RL J. Biol. Chem. 252:5142-5149(1977).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-329 OF MUTANT GLY-277.
RX PubMed=2204627; DOI=10.1016/s0021-9258(17)46264-8;
RA Vermersch P.S., Tesmer J.J.G., Lemon D.D., Quiocho F.A.;
RT "A Pro to Gly mutation in the hinge of the arabinose-binding protein
RT enhances binding and alters specificity. Sugar-binding and crystallographic
RT studies.";
RL J. Biol. Chem. 265:16592-16603(1990).
CC -!- FUNCTION: Involved in the high-affinity L-arabinose membrane transport
CC system. Binds with high affinity to arabinose, but can also bind D-
CC galactose (approximately 2-fold reduction) and D-fucose (approximately
CC 40-fold reduction).
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Induced by arabinose. Transcription is dependent on the
CC transcription factor AraC, the cAMP receptor protein (CRP) and cAMP.
CC {ECO:0000269|PubMed:2231717}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X06091; CAA29476.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74971.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15721.1; -; Genomic_DNA.
DR EMBL; K00420; AAA23472.1; -; Genomic_DNA.
DR PIR; E64953; JGECA.
DR RefSeq; NP_416414.1; NC_000913.3.
DR RefSeq; WP_000548675.1; NZ_STEB01000026.1.
DR PDB; 1ABE; X-ray; 1.70 A; A=24-329.
DR PDB; 1ABF; X-ray; 1.90 A; A=24-329.
DR PDB; 1APB; X-ray; 1.76 A; A=24-329.
DR PDB; 1BAP; X-ray; 1.75 A; A=24-329.
DR PDB; 2WRZ; X-ray; 2.20 A; A/B=24-329.
DR PDB; 5ABP; X-ray; 1.80 A; A=24-329.
DR PDB; 6ABP; X-ray; 1.67 A; A=24-329.
DR PDB; 7ABP; X-ray; 1.67 A; A=24-329.
DR PDB; 8ABP; X-ray; 1.49 A; A=24-329.
DR PDB; 9ABP; X-ray; 1.97 A; A=24-329.
DR PDBsum; 1ABE; -.
DR PDBsum; 1ABF; -.
DR PDBsum; 1APB; -.
DR PDBsum; 1BAP; -.
DR PDBsum; 2WRZ; -.
DR PDBsum; 5ABP; -.
DR PDBsum; 6ABP; -.
DR PDBsum; 7ABP; -.
DR PDBsum; 8ABP; -.
DR PDBsum; 9ABP; -.
DR AlphaFoldDB; P02924; -.
DR BMRB; P02924; -.
DR SMR; P02924; -.
DR BioGRID; 4261850; 21.
DR ComplexPortal; CPX-4314; Arabinose ABC transporter complex.
DR IntAct; P02924; 6.
DR STRING; 511145.b1901; -.
DR DrugBank; DB03485; alpha-D-Fucopyranose.
DR DrugBank; DB03142; Alpha-L-Arabinose.
DR DrugBank; DB04062; beta-D-fucose.
DR DrugBank; DB03246; Beta-L-Arabinose.
DR TCDB; 3.A.1.2.2; the atp-binding cassette (abc) superfamily.
DR jPOST; P02924; -.
DR PaxDb; P02924; -.
DR PRIDE; P02924; -.
DR EnsemblBacteria; AAC74971; AAC74971; b1901.
DR EnsemblBacteria; BAA15721; BAA15721; BAA15721.
DR GeneID; 66674211; -.
DR GeneID; 946409; -.
DR KEGG; ecj:JW1889; -.
DR KEGG; eco:b1901; -.
DR PATRIC; fig|1411691.4.peg.349; -.
DR EchoBASE; EB0055; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_046821_1_0_6; -.
DR OMA; EWKFADQ; -.
DR PhylomeDB; P02924; -.
DR BioCyc; EcoCyc:ARAF-MON; -.
DR BioCyc; MetaCyc:ARAF-MON; -.
DR EvolutionaryTrace; P02924; -.
DR PRO; PR:P02924; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0015407; F:ABC-type monosaccharide transporter activity; IMP:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IDA:EcoCyc.
DR GO; GO:0042882; P:L-arabinose transmembrane transport; IC:ComplexPortal.
DR CDD; cd01540; PBP1_arabinose_binding; 1.
DR InterPro; IPR026266; AraF.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR PIRSF; PIRSF002816; AraF; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:326784,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 24..329
FT /note="L-arabinose-binding periplasmic protein"
FT /id="PRO_0000031720"
FT SITE 87
FT /note="The binding site for the sugar molecule has not yet
FT been established, but C-87 may be involved"
FT MUTAGEN 277
FT /note="P->G: Improves binding to galactose."
FT CONFLICT 194
FT /note="Q -> E (in Ref. 1; CAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="V -> L (in Ref. 1; CAA29476)"
FT /evidence="ECO:0000305"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:8ABP"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:8ABP"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:8ABP"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:8ABP"
SQ SEQUENCE 329 AA; 35541 MW; A79D167EA92B0C64 CRC64;
MHKFTKALAA IGLAAVMSQS AMAENLKLGF LVKQPEEPWF QTEWKFADKA GKDLGFEVIK
IAVPDGEKTL NAIDSLAASG AKGFVICTPD PKLGSAIVAK ARGYDMKVIA VDDQFVNAKG
KPMDTVPLVM MAATKIGERQ GQELYKEMQK RGWDVKESAV MAITANELDT ARRRTTGSMD
ALKAAGFPEK QIYQVPTKSN DIPGAFDAAN SMLVQHPEVK HWLIVGMNDS TVLGGVRATE
GQGFKAADII GIGINGVDAV SELSKAQATG FYGSLLPSPD VHGYKSSEML YNWVAKDVEP
PKFTEVTDVV LITRDNFKEE LEKKGLGGK
