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Protein

ATP-dependent protease ATPase subunit HslU

Gene

hslU

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

Functioni

ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.7 Publications

Kineticsi

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.

  1. KM=0.31 mM for ATP (in the absence of HslV)2 Publications
  2. KM=0.28 mM for ATP (in the presence of HslV)2 Publications
  3. KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)2 Publications
  1. Vmax=57 pmol/min/mg enzyme (in the absence of HslV)2 Publications
  2. Vmax=213 pmol/min/mg enzyme (in the presence of HslV)2 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181ATP; via amide nitrogen and carbonyl oxygen
Binding sitei256 – 2561ATP
Binding sitei321 – 3211ATP
Binding sitei393 – 3931ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 656ATP

GO - Molecular functioni

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct
  • peptidase activity, acting on L-amino acid peptides Source: InterPro

GO - Biological processi

  • protein unfolding 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:EG11881-MONOMER.
ECOL316407:JW3902-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Heat shock protein HslU
Unfoldase HslU
Gene namesi
Name:hslU
Synonyms:htpI
Ordered Locus Names:b3931, JW3902
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11881. hslU.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • HslUV protease complex Source: UniProtKB-HAMAP
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631K → T: Can neither bind nor hydrolyze ATP. Do not form multimers, but stays as monomer. 1 Publication
Mutagenesisi80 – 801K → T: Some effect on protease activity. 1 Publication
Mutagenesisi88 – 881E → Q: Severly reduced protease activity. 1 Publication
Mutagenesisi91 – 911Y → G: Partial loss of protease activity. 1 Publication
Mutagenesisi92 – 921V → G: Partial loss of protease activity. 1 Publication
Mutagenesisi93 – 931G → A: Almost no protease or ATP hydrolysis activity. 1 Publication
Mutagenesisi95 – 951E → W: Partial loss of protease activity. 1 Publication
Mutagenesisi262 – 2621C → V: No effect on ATP hydrolysis. Can support HslV-mediated proteolysis at wild-type levels. 1 Publication
Mutagenesisi266 – 2661E → Q: No effect. 1 Publication
Mutagenesisi286 – 2861E → Q: Reduced protease activity. 1 Publication
Mutagenesisi288 – 2881C → V: No ATP hydrolysis activity. Binds ATP with lower affinity than wild-type. Can support HslV-mediated proteolysis to some extent. 1 Publication
Mutagenesisi312 – 3121I → W: No effect. 1 Publication
Mutagenesisi321 – 3211E → Q: Complete loss of activity. 1 Publication
Mutagenesisi325 – 3251R → E: Complete loss of activity. Forms wild-type complexes with HslV and is able to bind ATP. 1 Publication
Mutagenesisi385 – 3851E → K: No effect. 1 Publication
Mutagenesisi393 – 3931R → A: Complete loss of activity. 1 Publication
Mutagenesisi436 – 4361E → K: Partial loss of protease activity; when associated with K-437.
Mutagenesisi437 – 4371D → K: Partial loss of protease activity; when associated with K-436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443ATP-dependent protease ATPase subunit HslUPRO_0000160500Add
BLAST

Proteomic databases

EPDiP0A6H5.
PaxDbiP0A6H5.
PRIDEiP0A6H5.

2D gel databases

SWISS-2DPAGEP0A6H5.

Expressioni

Inductioni

By heat shock.1 Publication

Interactioni

Subunit structurei

A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-369317,EBI-369317
hslVP0A7B86EBI-369317,EBI-552265
sulAP0AFZ55EBI-369317,EBI-2012039

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261787. 209 interactions.
DIPiDIP-31855N.
IntActiP0A6H5. 46 interactions.
STRINGi511145.b3931.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 149Combined sources
Helixi21 – 3818Combined sources
Helixi42 – 476Combined sources
Beta strandi53 – 564Combined sources
Helixi63 – 719Combined sources
Turni72 – 754Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 908Combined sources
Helixi98 – 11316Combined sources
Turni114 – 1174Combined sources
Helixi118 – 1214Combined sources
Beta strandi124 – 1263Combined sources
Helixi127 – 1326Combined sources
Turni133 – 1353Combined sources
Helixi147 – 1493Combined sources
Turni150 – 1545Combined sources
Helixi155 – 1617Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi214 – 2163Combined sources
Helixi224 – 2329Combined sources
Helixi237 – 2404Combined sources
Helixi242 – 2509Combined sources
Beta strandi252 – 2565Combined sources
Helixi258 – 2614Combined sources
Helixi269 – 28618Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi295 – 2984Combined sources
Helixi299 – 3013Combined sources
Beta strandi303 – 3086Combined sources
Beta strandi311 – 3133Combined sources
Helixi315 – 3173Combined sources
Helixi320 – 3245Combined sources
Beta strandi328 – 3314Combined sources
Helixi337 – 3459Combined sources
Helixi351 – 36111Combined sources
Beta strandi365 – 3684Combined sources
Helixi370 – 38617Combined sources
Helixi393 – 40917Combined sources
Helixi410 – 4134Combined sources
Beta strandi417 – 4204Combined sources
Helixi422 – 43413Combined sources
Helixi436 – 4427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DO0X-ray3.00A/B/C/D/E/F2-443[»]
1DO2X-ray4.00A/B/C/D2-443[»]
1E94X-ray2.80E/F2-443[»]
1G4AX-ray3.00E/F1-443[»]
1G4BX-ray7.00E/F/K/L1-443[»]
1HQYX-ray2.80E/F2-443[»]
1HT1X-ray2.80E/F/G/I2-443[»]
1HT2X-ray2.80E/F/G/H2-443[»]
1YYFX-ray4.16A/B1-443[»]
DisProtiDP00100.
ProteinModelPortaliP0A6H5.
SMRiP0A6H5. Positions 1-443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6H5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family. HslU subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
HOGENOMiHOG000010036.
InParanoidiP0A6H5.
KOiK03667.
OMAiRLHTTIE.
OrthoDBiEOG6NPM7G.
PhylomeDBiP0A6H5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP
60 70 80 90 100
KNILMIGPTG VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII
110 120 130 140 150
RDLTDAAVKM VRVQAIEKNR YRAEELAEER ILDVLIPPAK NNWGQTEQQQ
160 170 180 190 200
EPSAARQAFR KKLREGQLDD KEIEIDLAAA PMGVEIMAPP GMEEMTSQLQ
210 220 230 240 250
SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK QDAIDAVEQH
260 270 280 290 300
GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
310 320 330 340 350
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS
360 370 380 390 400
ITVQYKALMA TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE
410 420 430 440
RLMEEISYDA SDLSGQNITI DADYVSKHLD ALVADEDLSR FIL
Length:443
Mass (Da):49,594
Last modified:March 29, 2005 - v1
Checksum:iD2188639EA9AEF4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.
PIRiJT0761.
RefSeqiNP_418366.1. NC_000913.3.
WP_001293341.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76913; AAC76913; b3931.
BAE77379; BAE77379; BAE77379.
GeneIDi948430.
KEGGiecj:JW3902.
eco:b3931.
PATRICi32123377. VBIEscCol129921_4049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.
PIRiJT0761.
RefSeqiNP_418366.1. NC_000913.3.
WP_001293341.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DO0X-ray3.00A/B/C/D/E/F2-443[»]
1DO2X-ray4.00A/B/C/D2-443[»]
1E94X-ray2.80E/F2-443[»]
1G4AX-ray3.00E/F1-443[»]
1G4BX-ray7.00E/F/K/L1-443[»]
1HQYX-ray2.80E/F2-443[»]
1HT1X-ray2.80E/F/G/I2-443[»]
1HT2X-ray2.80E/F/G/H2-443[»]
1YYFX-ray4.16A/B1-443[»]
DisProtiDP00100.
ProteinModelPortaliP0A6H5.
SMRiP0A6H5. Positions 1-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261787. 209 interactions.
DIPiDIP-31855N.
IntActiP0A6H5. 46 interactions.
STRINGi511145.b3931.

2D gel databases

SWISS-2DPAGEP0A6H5.

Proteomic databases

EPDiP0A6H5.
PaxDbiP0A6H5.
PRIDEiP0A6H5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76913; AAC76913; b3931.
BAE77379; BAE77379; BAE77379.
GeneIDi948430.
KEGGiecj:JW3902.
eco:b3931.
PATRICi32123377. VBIEscCol129921_4049.

Organism-specific databases

EchoBASEiEB1827.
EcoGeneiEG11881. hslU.

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
HOGENOMiHOG000010036.
InParanoidiP0A6H5.
KOiK03667.
OMAiRLHTTIE.
OrthoDBiEOG6NPM7G.
PhylomeDBiP0A6H5.

Enzyme and pathway databases

BioCyciEcoCyc:EG11881-MONOMER.
ECOL316407:JW3902-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6H5.
PROiP0A6H5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli."
    Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R.
    Gene 134:1-6(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    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. "Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli."
    Shin D.H., Yoo S.J., Shim Y.K., Seol J.H., Kang M.S., Chung C.H.
    FEBS Lett. 398:151-154(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-63.
  6. "Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli."
    Yoo S.J., Seol J.H., Shin D.H., Rohrwild M., Kang M.-S., Tanaka K., Goldberg A.L., Chung C.H.
    J. Biol. Chem. 271:14035-14040(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome."
    Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., Seol J.H., Chung C.H., Goldberg A.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli."
    Yoo S.J., Seol J.H., Seong I.S., Kang M.-S., Chung C.H.
    Biochem. Biophys. Res. Commun. 238:581-585(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECTS OF ATP BINDING ON COMPLEX FORMATION.
  9. "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.
  10. "The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase."
    Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L., Chung C.H.
    Eur. J. Biochem. 247:1143-1150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  11. "Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli."
    Kanemori M., Nishihara K., Yanagi H., Yura T.
    J. Bacteriol. 179:7219-7225(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  12. "Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis."
    Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H., Shimbara N., Tanaka K., Chung C.H.
    J. Biol. Chem. 273:22929-22935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-262 AND CYS-288.
  13. "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli."
    Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.
    FEBS Lett. 456:211-214(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  14. "Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation."
    Kanemori M., Yanagi H., Yura T.
    J. Biol. Chem. 274:22002-22007(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.
  15. "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease."
    Burton R.E., Baker T.A., Sauer R.T.
    Nat. Struct. Mol. Biol. 12:245-251(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis."
    Lee J.W., Park E., Jeong M.S., Jeon Y.J., Eom S.H., Seol J.H., Chung C.H.
    J. Biol. Chem. 284:33475-33484(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTION MECHANISM.
  17. "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH ATP AND HSLV.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176 OF APOENZYME AND IN COMPLEXES WITH HSLV AND ATP, MUTAGENESIS OF LYS-80; GLU-88; TYR-91; VAL-92; GLY-93; GLU-95; GLU-266; GLU-286; ILE-312; GLU-321; ARG-325; GLU-385 AND ARG-393.
  19. "Nucleotide-dependent conformational changes in a protease-associated ATPase HslU."
    Wang J., Song J.J., Seong I.S., Franklin M.C., Kamtekar S., Eom S.H., Chung C.H.
    Structure 9:1107-1116(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-443 IN COMPLEX WITH ADP.
  20. "Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects."
    Wang J., Rho S.H., Park H.H., Eom S.H.
    Acta Crystallogr. D 61:932-941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.16 ANGSTROMS) IN COMPLEX WITH B.SUBTILIS HSLV AND ADP.

Entry informationi

Entry nameiHSLU_ECOLI
AccessioniPrimary (citable) accession number: P0A6H5
Secondary accession number(s): P32168, Q2M8M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: March 16, 2016
This is version 105 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, 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.