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P54745 (HRSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heat-responsive suppressor hrsA
Alternative name(s):
Putative PTS system EIIABC component

Including the following 3 domains:

  1. Phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system EIIA component
  2. Phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system EIIB component
  3. Permease IIC component
    Alternative name(s):
    PTS system EIIC component
Gene names
Name:hrsA
Ordered Locus Names:b0731, JW0720
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in thermoinduction of ompC.

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane By similarity.

Catalytic activity

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

Sequence similarities

Contains 1 PTS EIIA type-2 domain.

Contains 1 PTS EIIB type-2 domain.

Contains 1 PTS EIIC type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 658658Heat-responsive suppressor hrsA
PRO_0000186699

Regions

Topological domain1 – 313313Periplasmic Potential
Transmembrane314 – 33421Helical; Potential
Topological domain335 – 35824Cytoplasmic Potential
Transmembrane359 – 37921Helical; Potential
Topological domain380 – 38910Periplasmic Potential
Transmembrane390 – 41021Helical; Potential
Topological domain411 – 43323Cytoplasmic Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 47420Periplasmic Potential
Transmembrane475 – 49521Helical; Potential
Topological domain496 – 5005Cytoplasmic Potential
Transmembrane501 – 52121Helical; Potential
Topological domain522 – 55130Periplasmic Potential
Transmembrane552 – 57221Helical; Potential
Topological domain5731Cytoplasmic Potential
Transmembrane574 – 59421Helical; Potential
Topological domain595 – 62026Periplasmic Potential
Transmembrane621 – 64121Helical; Potential
Topological domain642 – 65817Cytoplasmic Potential
Domain25 – 171147PTS EIIA type-2
Domain186 – 28297PTS EIIB type-2
Domain306 – 641336PTS EIIC type-2

Sites

Active site871Tele-phosphohistidine intermediate; for EIIA activity By similarity
Active site1921Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P54745 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C1F0999A1C48C5C2

FASTA65869,668
        10         20         30         40         50         60 
MVLFYRAHWR DYKNDQVRIM MNLTTLTHRD ALCLNARFTS REEAIHALTQ RLAALGKISS 

        70         80         90        100        110        120 
TEQFLEEVYR RESLGPTALG EGLAVPHGKT AAVKEAAFAV ATLSEPLQWE GVDGPEAVDL 

       130        140        150        160        170        180 
VVLLAIPPNE AGTTHMQLLT ALTTRLADDE IRARIQSATT PDELLSALDD KGGTQPSASF 

       190        200        210        220        230        240 
SNAPTIVCVT ACPAGIAHTY MAAEYLEKAG RKLGVNVYVE KQGANGIEGR LTADQLNSAT 

       250        260        270        280        290        300 
ACIFAAEVAI KESERFNGIP ALSVPVAEPI RHAEALIQQA LTLKRSDETR TVQQDTQPVK 

       310        320        330        340        350        360 
SVKTELKQAL LSGISFAVPL IVAGGTVLAV AVLLSQIFGL QDLFNEENSW LWMYRKLGGG 

       370        380        390        400        410        420 
LLGILMVPVL AAYTAYSLAD KPALAPGFAA GLAANMIGSG FLGAVVGGLI AGYLMRWVKN 

       430        440        450        460        470        480 
HLRLSSKFNG FLTFYLYPVL GTLGAGSLML FVVGEPVAWI NNSLTAWLNG LSGSNALLLG 

       490        500        510        520        530        540 
AILGFMCSFD LGGPVNKAAY AFCLGAMANG VYGPYAIFAS VKMVSAFTVT ASTMLAPRLF 

       550        560        570        580        590        600 
KEFEIETGKS TWLLGLAGIT EGAIPMAIED PLRVIGSFVL GSMVTGAIVG AMNIGLSTPG 

       610        620        630        640        650 
AGIFSLFLLH DNGAGGVMAA IGWFGAALVG AAISTAILLM WRRHAVKHGN YLTDGVMP 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the heat-responsive genes in Escherichia coli."
Utsumi R., Horie T., Katoh A., Kaino Y., Tanabe H., Noda M.
Biosci. Biotechnol. Biochem. 60:309-315(1996) [PubMed: 9063979] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 277-658.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D64014 Genomic DNA. Translation: BAA10893.1.
U00096 Genomic DNA. Translation: AAC73825.1.
AP009048 Genomic DNA. Translation: BAA35397.2.
PIRJC4598.
RefSeqNP_415259.1. NC_000913.2.

3D structure databases

ProteinModelPortalP54745.
SMRP54745. Positions 27-172, 183-287.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9939N.
IntActP54745. 1 interaction.
MINTMINT-1249398.

Protein family/group databases

TCDB4.A.2.1.3. PTS fructose-mannitol (Fru) family.

Proteomic databases

PRIDEP54745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000002928; EBESCP00000002928; EBESCG00000002393.
EBESCT00000017038; EBESCP00000016329; EBESCG00000016097.
GeneID945355.
GenomeReviewsGene locus JW0720 in contig AP009048_GR.
Gene locus b0731 in contig U00096_GR.
KEGGecj:JW0720.
eco:b0731.
PATRIC32116657. VBIEscCol129921_0761.

Organism-specific databases

EchoBASEEB3024.
EcoGeneEG13235. hrsA.

Phylogenomic databases

eggNOGCOG1299.
GeneTreeEBGT00070000031702.
HOGENOMHBG704192.
OMAMVSFDLG.
PhylomeDBP54745.
ProtClustDBPRK09765.

Enzyme and pathway databases

BioCycEcoCyc:HRSA-MONOMER.

Gene expression databases

GenevestigatorP54745.

Family and domain databases

InterProIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
Gene3DG3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
KOK11198.
K11199.
K11200.
PfamPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMSSF55804. PTrfase/Anion_transptr. 1 hit.
TIGRFAMsTIGR00829. FRU. 1 hit.
TIGR00848. FruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHRSA_ECOLI
AccessionPrimary (citable) accession number: P54745
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families