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Escherichia coli K-12 substr. MG1655 Transporter: xanthine:H+ symporter XanQ



Gene: xanQ Accession Numbers: G7501 (EcoCyc), b2882, ECK2878

Synonyms: ygfO, xanthine NCS2 transporter

Regulation Summary Diagram: ?

Summary:
XanQ (formerly YgfO) is a member of the NCS2 (Nucleobase-Cation Symport-2) family of transporters. XanQ is a specific, high-affinity, proton motive force-dependent xanthine transporter with a Km of 4.2 to 4.6 μM [Karatza05]. XanQ is unable to transport guanine, hypoxanthine, uric acid, and uracil, or to efficiently recognize certain xanthine or uric acid analogues [Karatza05]. XanQ is believed to be controlled by a σ54- dependent promoter [Xi00]. Cysteine scanning and site-directed mutagenesis has been performed [Karatza06, Papakostas08, Karena09].

Locations: inner membrane

Map Position: [3,022,373 -> 3,023,773] (65.14 centisomes)
Length: 1401 bp / 466 aa

Molecular Weight of Polypeptide: 49.108 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009463 , EchoBASE:EB2877 , EcoGene:EG13065 , EcoliWiki:b2882 , OU-Microarray:b2882 , PortEco:xanQ , Protein Model Portal:P67444 , RefSeq:NP_417358 , RegulonDB:G7501 , SMR:P67444 , String:511145.b2882 , UniProt:P67444

Relationship Links: InterPro:IN-FAMILY:IPR006042 , InterPro:IN-FAMILY:IPR006043 , Panther:IN-FAMILY:PTHR11119 , Pfam:IN-FAMILY:PF00860 , Prosite:IN-FAMILY:PS01116

In Paralogous Gene Group: 466 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0042906 - xanthine transport Inferred from experiment [Karatza05]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0055085 - transmembrane transport Inferred by computational analysis [GOA01]
Molecular Function: GO:0042907 - xanthine transmembrane transporter activity Inferred from experiment [Karatza05]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Karatza05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
transport Electrochemical potential driven transporters Porters (Uni-, Sym- and Antiporters)

Essentiality data for xanQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Last-Curated ? 03-Jan-2010 by Mackie A , Macquarie University


Enzymatic reaction of: xanthine:H+ symporter XanQ

Kinetic Parameters:

Substrate
Km (μM)
Citations
xanthine
4.6
[Karatza05]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 26 -> 46
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 31
[Karena09, UniProt11]
Alternate sequence: H → Q; UniProt: Increase of activity.
Alternate sequence: H → N; UniProt: No change in activity.
Alternate sequence: H → R; UniProt: Strong decrease in activity.
Alternate sequence: H → K; UniProt: Strong decrease in activity.
Alternate sequence: H → L; UniProt: Decrease in activity.
Alternate sequence: H → C; UniProt: Decrease in activity.
Amino-Acid-Site 31
[UniProt10a]
UniProt: Essential for affinity and specificity; Sequence Annotation Type: site;
Transmembrane-Region 56 -> 76
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 81 -> 101
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 93
[Karena09, UniProt11]
Alternate sequence: N → S; UniProt: Increase of activity.
Alternate sequence: N → Q; UniProt: Loss of activity.
Alternate sequence: N → T; UniProt: Strong decrease in activity.
Alternate sequence: N → D; UniProt: Strong decrease in activity.
Alternate sequence: N → C; UniProt: Strong decrease in activity.
Alternate sequence: N → A; UniProt: Highly active.
Amino-Acid-Site 93
[UniProt10a]
UniProt: Essential for affinity and specificity; Sequence Annotation Type: site;
Transmembrane-Region 121 -> 141
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 152 -> 172
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 164
[Karena09, UniProt11]
Alternate sequence: K → R; UniProt: Highly active.
Alternate sequence: K → C; UniProt: Highly active.
Transmembrane-Region 181 -> 201
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 211 -> 231
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 232
[Karena09, UniProt11]
Alternate sequence: D → E; UniProt: Highly active.
Alternate sequence: D → C; UniProt: Decrease in activity.
Mutagenesis-Variant 258
[Karena09, UniProt11]
Alternate sequence: Q → N; UniProt: Highly active.
Alternate sequence: Q → C; UniProt: Decrease in activity.
Transmembrane-Region 259 -> 279
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 272
[Karena09, UniProt11]
Alternate sequence: E → D; UniProt: Strong decrease in activity.
Alternate sequence: E → C; UniProt: Loss of activity.
Amino-Acid-Site 272
[UniProt10a]
UniProt: Essential for purine uptake; Sequence Annotation Type: site;
Transmembrane-Region 299 -> 319
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 304
[Karena09, UniProt11]
Alternate sequence: D → E; UniProt: Strong decrease in activity.
Alternate sequence: D → C; UniProt: Loss of activity.
Amino-Acid-Site 304
[UniProt10a]
UniProt: Essential for purine uptake; Sequence Annotation Type: site;
Transmembrane-Region 343 -> 363
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 365 -> 384
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 385
[Karena09, UniProt11]
Alternate sequence: R → K; UniProt: Highly active.
Alternate sequence: R → C; UniProt: Decrease in activity.
Mutagenesis-Variant 421
[Papakostas08, UniProt11]
Alternate sequence: P → G; UniProt: Highly active.
Alternate sequence: P → C; UniProt: Strong decrease in activity.
Mutagenesis-Variant 423
[Papakostas08, UniProt11]
Alternate sequence: S → C; UniProt: Highly active.
Mutagenesis-Variant 424
[Papakostas08, UniProt11]
Alternate sequence: I → C; UniProt: Highly active.
Mutagenesis-Variant 425
[Papakostas08, UniProt11]
Alternate sequence: Y → C; UniProt: Strong decrease in activity.
Transmembrane-Region 426 -> 446
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 427
[Papakostas08, UniProt11]
Alternate sequence: L → C; UniProt: Decrease in activity.
Mutagenesis-Variant 430
[Papakostas08, UniProt11]
Alternate sequence: N → T; UniProt: Loss of activity.
Amino-Acid-Site 430
[UniProt10a]
UniProt: Important for purine uptake and affinity; Sequence Annotation Type: site;
Mutagenesis-Variant 432
[Papakostas08, UniProt11]
Alternate sequence: I → Q; UniProt: Highly active.
Alternate sequence: I → N; UniProt: Highly active.
Alternate sequence: I → F; UniProt: Loss of activity.
Alternate sequence: I → E; UniProt: Loss of activity.
Alternate sequence: I → M; UniProt: Loss of activity.
Alternate sequence: I → L; UniProt: Loss of activity.
Alternate sequence: I → V; UniProt: Strong decrease in activity.
Alternate sequence: I → T; UniProt: Strong decrease in activity.
Alternate sequence: I → S; UniProt: Strong decrease in activity.
Alternate sequence: I → A; UniProt: Strong decrease in activity.
Amino-Acid-Site 432
[UniProt10a]
UniProt: Important for purine uptake and affinity; Sequence Annotation Type: site;
Mutagenesis-Variant 436
[Papakostas08, UniProt11]
Alternate sequence: G → C; UniProt: Highly active.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Karatza05: Karatza P, Frillingos S (2005). "Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli." Mol Membr Biol 22(3);251-61. PMID: 16096267

Karatza06: Karatza P, Panos P, Georgopoulou E, Frillingos S (2006). "Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an alpha-helix." J Biol Chem 281(52);39881-90. PMID: 17077086

Karena09: Karena E, Frillingos S (2009). "Role of intramembrane polar residues in the YgfO xanthine permease: HIS-31 and ASN-93 are crucial for affinity and specificity, and ASP-304 and GLU-272 are irreplaceable." J Biol Chem 284(36);24257-68. PMID: 19581302

Papakostas08: Papakostas K, Georgopoulou E, Frillingos S (2008). "Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: ILE-432 and ASN-430 are important." J Biol Chem 283(20);13666-78. PMID: 18359771

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Xi00: Xi H, Schneider BL, Reitzer L (2000). "Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage." J Bacteriol 182(19);5332-41. PMID: 10986234


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC13A.