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P0AFZ7 (TRKH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trk system potassium uptake protein TrkH
Gene names
Name:trkH
Ordered Locus Names:b3849, JW5576
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA and requires TrkE for transport activity.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.7.

Sequence similarities

Belongs to the TrkH potassium transport family.

Sequence caution

The sequence AAA67646.1 differs from that shown. Reason: Frameshift at position 416.

The sequence X54687 differs from that shown. Reason: Frameshift at positions 418 and 420.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Trk system potassium uptake protein TrkH
PRO_0000070475

Regions

Topological domain1 – 22Cytoplasmic By similarity
Transmembrane3 – 2927Helical; By similarity
Topological domain30 – 356Periplasmic By similarity
Transmembrane36 – 5722Helical; By similarity
Topological domain58 – 658Cytoplasmic By similarity
Transmembrane66 – 9025Helical; By similarity
Topological domain91 – ?Periplasmic By similarity
Intramembrane? – 97 By similarity
Intramembrane98 – 10912Helical; Pore-forming; By similarity
Intramembrane110 – 1156 By similarity
Topological domain116 – 1249Periplasmic By similarity
Transmembrane125 – 15026Helical; By similarity
Topological domain151 – 17727Cytoplasmic By similarity
Transmembrane178 – 20225Helical; By similarity
Topological domain203 – 2053Periplasmic By similarity
Intramembrane2061 By similarity
Intramembrane207 – 21812Helical; Pore-forming; By similarity
Intramembrane219 – 2246 By similarity
Topological domain225 – 23410Periplasmic By similarity
Intramembrane235 – 25016Helical; By similarity
Intramembrane251 – ? By similarity
Topological domain? – 273Cytoplasmic By similarity
Transmembrane274 – 29421Helical; By similarity
Topological domain295 – ?Periplasmic By similarity
Intramembrane? – 300 By similarity
Intramembrane301 – 31616Helical; Pore-forming; By similarity
Intramembrane317 – 3226 By similarity
Topological domain323 – 3308Periplasmic By similarity
Intramembrane331 – 34212Helical; By similarity
Intramembrane343 – 35513Note=Loop between two helices; By similarity
Intramembrane356 – ?Helical; By similarity
Topological domain? – 389Cytoplasmic By similarity
Transmembrane390 – 41728Helical; By similarity
Topological domain418 – 4192Periplasmic By similarity
Intramembrane420 – 4212 By similarity
Intramembrane422 – 43211Helical; Pore-forming; By similarity
Intramembrane433 – 4397 By similarity
Topological domain440 – 45112Periplasmic By similarity
Intramembrane452 – 46312Helical; By similarity
Intramembrane464 – ? By similarity
Topological domain? – 483Cytoplasmic By similarity
Region110 – 1156Selectivity filter part 1 By similarity
Region219 – 2246Selectivity filter part 2 By similarity
Region317 – 3226Selectivity filter part 3 By similarity
Region434 – 4396Selectivity filter part 4 By similarity

Sites

Binding site1111Potassium ion; via carbonyl oxygen By similarity
Binding site1121Potassium ion; via carbonyl oxygen By similarity
Binding site2211Potassium ion; via carbonyl oxygen By similarity
Binding site4351Potassium ion; via carbonyl oxygen By similarity

Experimental info

Sequence conflict691Missing in AAA67646. Ref.3
Sequence conflict1441V → IV in X54687. Ref.1
Sequence conflict1961C → S in X54687. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0AFZ7 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 1AA9CC2F83EB509A

FASTA48352,960
        10         20         30         40         50         60 
MHFRAITRIV GLLVILFSGT MIIPGLVALI YRDGAGRAFT QTFFVALAIG SMLWWPNRKE 

        70         80         90        100        110        120 
KGELKSREGF LIVVLFWTVL GSVGALPFIF SESPNLTITD AFFESFSGLT TTGATTLVGL 

       130        140        150        160        170        180 
DSLPHAILFY RQMLQWFGGM GIIVLAVAIL PILGVGGMQL YRAEMPGPLK DNKMRPRIAE 

       190        200        210        220        230        240 
TAKTLWLIYV LLTVACALAL WFAGMDAFDA IGHSFATIAI GGFSTHDASI GYFDSPTINT 

       250        260        270        280        290        300 
IIAIFLLISG CNYGLHFSLL SGRSLKVYWR DPEFRMFIGV QFTLVVICTL VLWFHNVYSS 

       310        320        330        340        350        360 
ALMTINQAFF QVVSMATTAG FTTDSIARWP LFLPVLLLCS AFIGGCAGST GGGLKVIRIL 

       370        380        390        400        410        420 
LLFKQGNREL KRLVHPNAVY SIKLGNRALP ERILEAVWGF FSAYALVFIV SMLAIIATGV 

       430        440        450        460        470        480 
DDFSAFASVV ATLNNLGPGL GVVADNFTSM NPVAKWILIA NMLFGRLEVF TLLVLFTPTF 


WRE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli."
Nakahigashi K., Inokuchi H.
Nucleic Acids Res. 18:6439-6439(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"TrkH and its homolog, TrkG, determine the specificity and kinetics of cation transport by the Trk system of Escherichia coli."
Schlosser A., Meldorf M., Stumpe S., Bakker E.P., Epstein W.
J. Bacteriol. 177:1908-1910(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 69.
Strain: K12 / MG1655 / ATCC 47076.
[5]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54687 Genomic DNA. No translation available.
M87049 Genomic DNA. Translation: AAA67646.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48231.1.
AP009048 Genomic DNA. Translation: BAE77454.1.
PIRB65190.
RefSeqYP_026273.1. NC_000913.3.
YP_491595.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AFZ7.
SMRP0AFZ7. Positions 1-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47978N.
IntActP0AFZ7. 2 interactions.
MINTMINT-1238565.
STRING511145.b3849.

Protein family/group databases

TCDB2.A.38.1.1. the k(+) transporter (trk) family.

Proteomic databases

PRIDEP0AFZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48231; AAT48231; b3849.
BAE77454; BAE77454; BAE77454.
GeneID12933625.
948333.
KEGGecj:Y75_p3331.
eco:b3849.
PATRIC32123195. VBIEscCol129921_3963.

Organism-specific databases

EchoBASEEB1014.
EcoGeneEG11021. trkH.

Phylogenomic databases

eggNOGCOG0168.
HOGENOMHOG000225541.
KOK03498.
OMAYRHLLQW.
OrthoDBEOG63589N.
PhylomeDBP0AFZ7.
ProtClustDBPRK10750.

Enzyme and pathway databases

BioCycEcoCyc:TRKH-MONOMER.
ECOL316407:JW5576-MONOMER.

Gene expression databases

GenevestigatorP0AFZ7.

Family and domain databases

InterProIPR003445. Cat_transpt.
IPR004772. K_uptake_TrkH_fam.
[Graphical view]
PfamPF02386. TrkH. 1 hit.
[Graphical view]
PIRSFPIRSF006247. TrkH. 1 hit.
TIGRFAMsTIGR00933. 2a38. 1 hit.
ProtoNetSearch...

Other

PROP0AFZ7.

Entry information

Entry nameTRKH_ECOLI
AccessionPrimary (citable) accession number: P0AFZ7
Secondary accession number(s): P21166, P76769, Q2M8F2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene