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Protein

Chaperone protein HtpG

Gene

htpG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone. Has ATPase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATP1 Publication
Binding sitei80 – 801ATP1 Publication
Binding sitei127 – 1271ATP; via amide nitrogen1 Publication
Binding sitei174 – 1741ATP1 Publication
Binding sitei255 – 2551ATP1 Publication

GO - Molecular functioni

  • ATPase activity Source: CACAO
  • ATPase activity, coupled Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • protein folding Source: EcoCyc
  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10461-MONOMER.
ECOL316407:JW0462-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein HtpG
Alternative name(s):
Heat shock protein C62.5
Heat shock protein HtpG
High temperature protein G
Gene namesi
Name:htpG
Ordered Locus Names:b0473, JW0462
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10461. htpG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 624624Chaperone protein HtpGPRO_0000062985Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP0A6Z3.
PaxDbiP0A6Z3.
PRIDEiP0A6Z3.

2D gel databases

SWISS-2DPAGEP0A6Z3.

Interactioni

Subunit structurei

Homodimer. Oligomerizes at 65 degrees Celsius.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-369221,EBI-369221
dnaKP0A6Y83EBI-369221,EBI-542092
rpoCP0A8T72EBI-369221,EBI-543604

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261971. 197 interactions.
DIPiDIP-29797N.
IntActiP0A6Z3. 61 interactions.
MINTiMINT-1227806.
STRINGi511145.b0473.

Structurei

Secondary structure

1
624
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi11 – 2313Combined sources
Helixi25 – 295Combined sources
Helixi30 – 5021Combined sources
Helixi54 – 574Combined sources
Beta strandi65 – 706Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 806Combined sources
Helixi87 – 948Combined sources
Helixi102 – 1087Combined sources
Helixi113 – 1208Combined sources
Helixi127 – 1326Combined sources
Beta strandi134 – 1429Combined sources
Beta strandi144 – 1463Combined sources
Helixi148 – 1503Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi158 – 16710Combined sources
Beta strandi173 – 1808Combined sources
Helixi185 – 1884Combined sources
Helixi190 – 20011Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi221 – 2266Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 2403Combined sources
Helixi243 – 25412Combined sources
Beta strandi261 – 2688Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2807Combined sources
Turni286 – 2894Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi304 – 3107Combined sources
Helixi311 – 3133Combined sources
Helixi316 – 3183Combined sources
Beta strandi322 – 3309Combined sources
Helixi336 – 3416Combined sources
Helixi343 – 36624Combined sources
Helixi368 – 38215Combined sources
Helixi385 – 3884Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 3975Combined sources
Beta strandi402 – 4043Combined sources
Turni405 – 4084Combined sources
Helixi416 – 4216Combined sources
Beta strandi429 – 4346Combined sources
Helixi438 – 4425Combined sources
Helixi445 – 4473Combined sources
Helixi448 – 4536Combined sources
Beta strandi457 – 4604Combined sources
Helixi465 – 4684Combined sources
Turni469 – 4713Combined sources
Beta strandi474 – 4774Combined sources
Beta strandi478 – 4825Combined sources
Helixi488 – 4936Combined sources
Helixi511 – 5199Combined sources
Helixi520 – 5223Combined sources
Beta strandi523 – 5286Combined sources
Beta strandi537 – 5404Combined sources
Helixi548 – 5558Combined sources
Turni556 – 5583Combined sources
Beta strandi567 – 5704Combined sources
Helixi575 – 5828Combined sources
Helixi586 – 60520Combined sources
Helixi611 – 62313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SF8X-ray2.60A/B/C/D/E/F/G/H511-624[»]
1Y4SX-ray2.90A/B1-559[»]
1Y4UX-ray2.90A/B1-559[»]
2GQ0X-ray1.90A/B230-495[»]
2IOPX-ray3.55A/B/C/D1-624[»]
2IOQX-ray3.50A/B1-624[»]
2IORX-ray1.65A1-215[»]
ProteinModelPortaliP0A6Z3.
SMRiP0A6Z3. Positions 1-624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6Z3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 336336A; substrate-bindingAdd
BLAST
Regioni337 – 552216BAdd
BLAST
Regioni553 – 62472CAdd
BLAST
Regioni585 – 62440Mediates dimerizationAdd
BLAST

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiENOG4105CJX. Bacteria.
COG0326. LUCA.
HOGENOMiHOG000031989.
InParanoidiP0A6Z3.
KOiK04079.
OMAiYLRFMRG.
OrthoDBiEOG65TRNM.
PhylomeDBiP0A6Z3.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA
60 70 80 90 100
LSNPDLYEGD GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS
110 120 130 140 150
GTKSFLESLG SDQAKDSQLI GQFGVGFYSA FIVADKVTVR TRAAGEKPEN
160 170 180 190 200
GVFWESAGEG EYTVADITKE DRGTEITLHL REGEDEFLDD WRVRSIISKY
210 220 230 240 250
SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE ITDEEYKEFY
260 270 280 290 300
KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
310 320 330 340 350
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN
360 370 380 390 400
ALTKRVLQML EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL
410 420 430 440 450
RFASTHTDSS AQTVSLEDYV SRMKEGQEKI YYITADSYAA AKSSPHLELL
460 470 480 490 500
RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF QSVSKVDESL EKLADEVDES
510 520 530 540 550
AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS TDADEMSTQM
560 570 580 590 600
AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
610 620
LLAERGTLED PNLFIRRMNQ LLVS
Length:624
Mass (Da):71,423
Last modified:June 7, 2005 - v1
Checksum:i1410577B589ADBAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38777 Genomic DNA. Translation: AAA23460.1.
U82664 Genomic DNA. Translation: AAB40227.1.
U00096 Genomic DNA. Translation: AAC73575.1.
AP009048 Genomic DNA. Translation: BAE76252.1.
PIRiA28324. HHEC62.
RefSeqiNP_415006.1. NC_000913.3.
WP_000678201.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC73575; AAC73575; b0473.
BAE76252; BAE76252; BAE76252.
GeneIDi945099.
KEGGiecj:JW0462.
eco:b0473.
PATRICi32116103. VBIEscCol129921_0493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38777 Genomic DNA. Translation: AAA23460.1.
U82664 Genomic DNA. Translation: AAB40227.1.
U00096 Genomic DNA. Translation: AAC73575.1.
AP009048 Genomic DNA. Translation: BAE76252.1.
PIRiA28324. HHEC62.
RefSeqiNP_415006.1. NC_000913.3.
WP_000678201.1. NZ_CP014272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SF8X-ray2.60A/B/C/D/E/F/G/H511-624[»]
1Y4SX-ray2.90A/B1-559[»]
1Y4UX-ray2.90A/B1-559[»]
2GQ0X-ray1.90A/B230-495[»]
2IOPX-ray3.55A/B/C/D1-624[»]
2IOQX-ray3.50A/B1-624[»]
2IORX-ray1.65A1-215[»]
ProteinModelPortaliP0A6Z3.
SMRiP0A6Z3. Positions 1-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261971. 197 interactions.
DIPiDIP-29797N.
IntActiP0A6Z3. 61 interactions.
MINTiMINT-1227806.
STRINGi511145.b0473.

2D gel databases

SWISS-2DPAGEP0A6Z3.

Proteomic databases

EPDiP0A6Z3.
PaxDbiP0A6Z3.
PRIDEiP0A6Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73575; AAC73575; b0473.
BAE76252; BAE76252; BAE76252.
GeneIDi945099.
KEGGiecj:JW0462.
eco:b0473.
PATRICi32116103. VBIEscCol129921_0493.

Organism-specific databases

EchoBASEiEB0456.
EcoGeneiEG10461. htpG.

Phylogenomic databases

eggNOGiENOG4105CJX. Bacteria.
COG0326. LUCA.
HOGENOMiHOG000031989.
InParanoidiP0A6Z3.
KOiK04079.
OMAiYLRFMRG.
OrthoDBiEOG65TRNM.
PhylomeDBiP0A6Z3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10461-MONOMER.
ECOL316407:JW0462-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6Z3.
PROiP0A6Z3.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli."
    Bardwell J.C.A., Craig E.A.
    Proc. Natl. Acad. Sci. U.S.A. 84:5177-5181(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / EMG2.
  6. "Purification and properties of the Escherichia coli heat shock protein, HtpG."
    Spence J., Georgopoulos C.
    J. Biol. Chem. 264:4398-4403(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8, SUBUNIT, PHOSPHORYLATION.
  7. "Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases."
    Nadeau K., Das A., Walsh C.T.
    J. Biol. Chem. 268:1479-1487(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ATPASE ACTIVITY.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone."
    Nemoto T.K., Ono T., Kobayakawa T., Tanaka E., Baba T.T., Tanaka K., Takagi T., Gotoh T.
    Eur. J. Biochem. 268:5258-5269(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN STRUCTURE.
  10. "Substrate-binding characteristics of proteins in the 90 kDa heat shock protein family."
    Nemoto T.K., Ono T., Tanaka K.
    Biochem. J. 354:663-670(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN STRUCTURE.
  11. Cited for: SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  12. "The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site."
    Harris S.F., Shiau A.K., Agard D.A.
    Structure 12:1087-1097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 511-624, HOMODIMERIZATION.
  13. "Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding."
    Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., Ke H.
    Structure 13:579-590(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-559 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY.
  14. "Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements."
    Shiau A.K., Harris S.F., Southworth D.R., Agard D.A.
    Cell 127:329-340(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.

Entry informationi

Entry nameiHTPG_ECOLI
AccessioniPrimary (citable) accession number: P0A6Z3
Secondary accession number(s): P10413, Q2MBV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.