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2.A.1.7.1 L-Fucose:H⁺ symporter. The x-ray structure (3.1Å resolution) with an outward open, amphipathic cavity has been solved. Asp46 and Glu135 can undergo cycles of protonation (Dang et al., 2010).
Accession Number:	P11551
Protein Name:	FucP aka B2801
Length:	438
Molecular Weight:	47545.00
Species:	Escherichia coli [83333]
Number of TMSs:	12
Location¹ / Topology² / Orientation³:	Cell inner membrane¹ / Multi-pass membrane protein²
Substrate	hydron, L-fucopyranose

Structure:
RefSeq:	AP_003367.1 NP_417281.1
Entrez Gene ID:	947487
Pfam:	PF07690
BioCyc:	EcoCyc:FUCP-MONOMER ECOL168927:B2801-MONOMER
KEGG:	ecj:JW2772 eco:b2801
Gene Ontology GO:0016021 C:integral to membrane GO:0005886 C:plasma membrane GO:0015518 F:arabinose:hydrogen symporter activity GO:0015535 F:fucose:hydrogen symporter activity GO:0015517 F:galactose:hydrogen symporter activity GO:0015751 P:arabinose transport GO:0015755 P:fructose transport GO:0006004 P:fucose metabolic process GO:0015756 P:fucose transport GO:0015757 P:galactose transport GO:0055085 P:transmembrane transport
References (8) [1] “The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation.” Lu Z.et.al. 2664711 [2] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [4] “Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol.” Chen Y.M.et.al. 2553671 [5] “Identification of a novel sugar-H+ symport protein, FucP, for transport of L-fucose into Escherichia coli.” Gunn F.J.et.al. 8052131 [6] “Proton-linked L-fucose transport in Escherichia coli.” Bradley S.A.et.al. 2829831 [7] “Topological analyses of the L-fucose-H+ symport protein, FucP, from Escherichia coli.” Gunn F.J.et.al. 7783647 [8] “Global topology analysis of the Escherichia coli inner membrane proteome.” Daley D.O.et.al. 15919996
3O7P 3O7Q

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MGNTSIQTQS YRAVDKDAGQ SRSYIIPFAL LCSLFFLWAV ANNLNDILLP QFQQAFTLTN 
61:	FQAGLIQSAF YFGYFIIPIP AGILMKKLSY KAGIITGLFL YALGAALFWP AAEIMNYTLF 
121:	LVGLFIIAAG LGCLETAANP FVTVLGPESS GHFRLNLAQT FNSFGAIIAV VFGQSLILSN 
181:	VPHQSQDVLD KMSPEQLSAY KHSLVLSVQT PYMIIVAIVL LVALLIMLTK FPALQSDNHS 
241:	DAKQGSFSAS LSRLARIRHW RWAVLAQFCY VGAQTACWSY LIRYAVEEIP GMTAGFAANY 
301:	LTGTMVCFFI GRFTGTWLIS RFAPHKVLAA YALIAMALCL ISAFAGGHVG LIALTLCSAF 
361:	MSIQYPTIFS LGIKNLGQDT KYGSSFIVMT IIGGGIVTPV MGFVSDAAGN IPTAELIPAL 
421:	CFAVIFIFAR FRSQTATN

2.A.1.7.1
L-Fucose:H⁺ symporter. The x-ray structure (3.1Å resolution) with an outward open, amphipathic cavity has been solved. Asp46 and Glu135 can undergo cycles of protonation (Dang et al., 2010).

Cross database links:

Gene Ontology

References (8)

External Searches:

Analyze:

2.A.1.7.1L-Fucose:H+ symporter. The x-ray structure (3.1Å resolution) with an outward open, amphipathic cavity has been solved. Asp46 and Glu135 can undergo cycles of protonation (Dang et al., 2010).

Cross database links:

Gene Ontology

References (8)

External Searches:

Analyze:

2.A.1.7.1
L-Fucose:H⁺ symporter. The x-ray structure (3.1Å resolution) with an outward open, amphipathic cavity has been solved. Asp46 and Glu135 can undergo cycles of protonation (Dang et al., 2010).