araF

Functionⁱ

Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	87	The binding site for the sugar molecule has not yet been established, but C-87 may be involved		1

GO - Molecular functionⁱ

monosaccharide binding
Source: EcoCyc
Inferred from direct assayⁱ
- 338992
monosaccharide-transporting ATPase activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 6282256

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

L-arabinose transmembrane transport Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Sugar transport, Transport

Biological process

Sugar transport, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ARAF-MONOMER MetaCyc:ARAF-MONOMER

BioCycⁱ

EcoCyc:ARAF-MONOMER
MetaCyc:ARAF-MONOMER

Protein family/group databases

TCDBⁱ	3.A.1.2.2 the atp-binding cassette (abc) superfamily

TCDBⁱ

3.A.1.2.2 the atp-binding cassette (abc) superfamily

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: L-arabinose-binding periplasmic protein Short name: ABP
Gene namesⁱ	Name:araF Ordered Locus Names:b1901, JW1889
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10057 araF

EcoGeneⁱ

EG10057 araF

Subcellular locationⁱ

Periplasm

GO - Cellular componentⁱ

outer membrane-bounded periplasmic space
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Periplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	277	P → G: Improves binding to galactose.		1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03485 Alpha-D-Fucose DB03142 Alpha-L-Arabinose DB04062 Beta-D-Fucose DB03246 Beta-L-Arabinose

DrugBankⁱ

DB03485 Alpha-D-Fucose
DB03142 Alpha-L-Arabinose
DB04062 Beta-D-Fucose
DB03246 Beta-L-Arabinose

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 23	2 PublicationsAdd BLAST		23
ChainⁱPRO_0000031720	24 – 329	L-arabinose-binding periplasmic proteinAdd BLAST		306

Proteomic databases

EPDⁱ	P02924
PaxDbⁱ	P02924
PRIDEⁱ	P02924

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	4261850, 21 interactors
IntActⁱ	P02924, 5 interactors
STRINGⁱ	316385.ECDH10B_2041

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	26 – 33	Combined sources	8
Helixⁱ	38 – 54	Combined sources	17
Beta strandⁱ	56 – 62	Combined sources	7
Helixⁱ	66 – 78	Combined sources	13
Beta strandⁱ	83 – 87	Combined sources	5
Helixⁱ	91 – 93	Combined sources	3
Helixⁱ	94 – 103	Combined sources	10
Beta strandⁱ	107 – 113	Combined sources	7
Beta strandⁱ	128 – 131	Combined sources	4
Helixⁱ	133 – 151	Combined sources	19
Helixⁱ	155 – 157	Combined sources	3
Beta strandⁱ	158 – 164	Combined sources	7
Helixⁱ	169 – 185	Combined sources	17
Helixⁱ	189 – 191	Combined sources	3
Beta strandⁱ	192 – 196	Combined sources	5
Beta strandⁱ	198 – 201	Combined sources	4
Helixⁱ	202 – 213	Combined sources	12
Beta strandⁱ	220 – 225	Combined sources	6
Helixⁱ	229 – 241	Combined sources	13
Helixⁱ	246 – 248	Combined sources	3
Beta strandⁱ	249 – 256	Combined sources	8
Helixⁱ	257 – 259	Combined sources	3
Helixⁱ	260 – 263	Combined sources	4
Beta strandⁱ	265 – 267	Combined sources	3
Beta strandⁱ	270 – 276	Combined sources	7
Helixⁱ	279 – 296	Combined sources	18
Beta strandⁱ	302 – 306	Combined sources	5
Beta strandⁱ	310 – 313	Combined sources	4
Turnⁱ	314 – 316	Combined sources	3
Helixⁱ	317 – 323	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P02924
SMRⁱ	P02924
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P02924

EvolutionaryTraceⁱ

P02924

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the bacterial solute-binding protein 2 family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG4105DMK Bacteria COG1879 LUCA
HOGENOMⁱ	HOG000220638
KEGG Orthology (KO) More...KOⁱ	K10537
OMAⁱ	NDIPGAL
PhylomeDBⁱ	P02924

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01540 PBP1_arabinose_binding, 1 hit
InterProⁱ	View protein in InterPro IPR026266 AraF IPR001761 Peripla_BP/Lac1_sug-bd_dom IPR028082 Peripla_BP_I
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00532 Peripla_BP_1, 1 hit
PIRSFⁱ	PIRSF002816 AraF, 1 hit
SUPFAMⁱ	SSF53822 SSF53822, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P02924-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MHKFTKALAA IGLAAVMSQS AMAENLKLGF LVKQPEEPWF QTEWKFADKA 
        60         70         80         90        100
GKDLGFEVIK IAVPDGEKTL NAIDSLAASG AKGFVICTPD PKLGSAIVAK 
       110        120        130        140        150
ARGYDMKVIA VDDQFVNAKG KPMDTVPLVM MAATKIGERQ GQELYKEMQK 
       160        170        180        190        200
RGWDVKESAV MAITANELDT ARRRTTGSMD ALKAAGFPEK QIYQVPTKSN 
       210        220        230        240        250
DIPGAFDAAN SMLVQHPEVK HWLIVGMNDS TVLGGVRATE GQGFKAADII 
       260        270        280        290        300
GIGINGVDAV SELSKAQATG FYGSLLPSPD VHGYKSSEML YNWVAKDVEP 
       310        320 
PKFTEVTDVV LITRDNFKEE LEKKGLGGK

Length:329

Mass (Da):35,541

Last modified:November 1, 1997 - v2

Checksum:ⁱA79D167EA92B0C64

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	194	Q → E in CAA29476 (PubMed:2445996).Curated		1
Sequence conflictⁱ	281	V → L in CAA29476 (PubMed:2445996).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06091 Genomic DNA Translation: CAA29476.1 U00096 Genomic DNA Translation: AAC74971.1 AP009048 Genomic DNA Translation: BAA15721.1 K00420 Genomic DNA Translation: AAA23472.1
PIRⁱ	E64953 JGECA
NCBI Reference Sequences More...RefSeqⁱ	NP_416414.1, NC_000913.3 WP_000548675.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74971; AAC74971; b1901 BAA15721; BAA15721; BAA15721
GeneIDⁱ	946409
KEGGⁱ	ecj:JW1889 eco:b1901
PATRICⁱ	fig\|1411691.4.peg.349

Protein	Similar proteins		Species	Score	Length	Source
P02924	L-arabinose-binding periplasmic protein		ECOLX		346	UniRef100_P02924
L-arabinose-binding periplasmic protein		Escherichia coli 907672		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 145-7		346
L-arabinose-binding periplasmic protein		Escherichia coli 908525		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 117-3		346
+123

Protein	Similar proteins		Species	Score	Length	Source
P02924	L-arabinose-binding periplasmic protein		ECOLX		346	UniRef90_P02924
L-arabinose-binding periplasmic protein		Escherichia coli 907672		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 145-7		346
L-arabinose-binding periplasmic protein		Escherichia coli 908525		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 117-3		346
+342

Protein	Similar proteins		Species	Score	Length	Source
P02924	L-arabinose-binding periplasmic protein		ECOLX		346	UniRef50_P02924
L-arabinose-binding periplasmic protein		Escherichia coli 907672		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 145-7		346
L-arabinose-binding periplasmic protein		Escherichia coli 908525		346
L-arabinose-binding periplasmic protein		Escherichia coli MS 117-3		346
+2202

Entry informationⁱ

Entry nameⁱ	ARAF_ECOLI
Accessionⁱ	P02924Primary (citable) accession number: P02924
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	November 1, 1997
	Last modified:	April 25, 2018
	This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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UniParc

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Supporting data

UniProtKB - P02924 (ARAF_ECOLI)

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L-arabinose-binding periplasmic protein

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ