Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GTPase HflX

Gene

hflX

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

Functioni

GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. In vitro, also exhibits ATPase activity.UniRule annotation3 Publications

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Intrinsic GTPase activity is very slow and can be stimulated by the presence of 50S ribosomal subunits or 70S ribosomes. GTPase activity is inhibited by ATP.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi211 – 2111MagnesiumUniRule annotation
Metal bindingi231 – 2311MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2118GTPUniRule annotation
Nucleotide bindingi229 – 2335GTPUniRule annotation
Nucleotide bindingi251 – 2544GTPUniRule annotation
Nucleotide bindingi317 – 3204GTPUniRule annotation
Nucleotide bindingi343 – 3453GTPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: EcoliWiki
  • GTPase activity Source: UniProtKB-HAMAP
  • GTP binding Source: EcoCyc
  • magnesium ion binding Source: UniProtKB-HAMAP
  • ribosome binding Source: EcoCyc
  • rRNA binding Source: EcoCyc

GO - Biological processi

  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Ligandi

ATP-binding, GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10437-MONOMER.
ECOL316407:JW4131-MONOMER.
MetaCyc:EG10437-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase HflXUniRule annotation
Alternative name(s):
GTP-binding protein HflXUniRule annotation
Gene namesi
Name:hflXUniRule annotation
Ordered Locus Names:b4173, JW4131
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10437. hflX.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

  • Note: May associate with membranes.

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Disruption does not affect lambda lysogeny or the transposition frequency of transposable elements.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426GTPase HflXPRO_0000122463Add
BLAST

Proteomic databases

PaxDbiP25519.
PRIDEiP25519.

Interactioni

Subunit structurei

Monomer. Associates with the 50S ribosomal subunit. This interaction occurs in the presence of GTP, GDP, ATP or ADP, but not in their absence.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4261252. 360 interactions.
DIPiDIP-9895N.
IntActiP25519. 1 interaction.
STRINGi511145.b4173.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ADYelectron microscopy4.5061-426[»]
ProteinModelPortaliP25519.
SMRiP25519. Positions 50-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 365168Hflx-type GUniRule annotationAdd
BLAST

Domaini

Full-length protein is required for specific association with the 50S ribosomal subunit.1 Publication

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.UniRule annotation
Contains 1 Hflx-type G (guanine nucleotide-binding) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1N. Bacteria.
COG2262. LUCA.
HOGENOMiHOG000260368.
InParanoidiP25519.
KOiK03665.
OMAiAVLVHIN.
OrthoDBiEOG60SCM2.
PhylomeDBiP25519.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00900. GTPase_HflX.
InterProiIPR009022. EFG_III-V.
IPR030394. G_HFLX_dom.
IPR032305. GTP-bd_M.
IPR006073. GTP_binding_domain.
IPR016496. GTPase_HflX.
IPR025121. GTPase_HflX_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10229. PTHR10229. 1 hit.
PfamiPF16360. GTP-bdg_M. 1 hit.
PF13167. GTP-bdg_N. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF006809. GTP-binding_hflX_prd. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 1 hit.
TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
PROSITEiPS51705. G_HFLX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE ALQVITGSRK
60 70 80 90 100
APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV
110 120 130 140 150
IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI
160 170 180 190 200
GLRGPGETQL ETDRRLLRNR IVQIQSRLER VEKQREQGRQ SRIKADVPTV
210 220 230 240 250
SLVGYTNAGK STLFNRITEA RVYAADQLFA TLDPTLRRID VADVGETVLA
260 270 280 290 300
DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIEAVNT
310 320 330 340 350
VLEEIDAHEI PTLLVMNKID MLEDFEPRID RDEENKPNRV WLSAQTGAGI
360 370 380 390 400
PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV
410 420
SLQVRMPIVD WRRLCKQEPA LIDYLI
Length:426
Mass (Da):48,327
Last modified:February 1, 1994 - v3
Checksum:i8D0A5BE92EE32591
GO

Sequence cautioni

The sequence BAA00645.1 differs from that shown. Reason: Frameshift at position 18. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531H → R in BAA00645 (PubMed:2020545).Curated
Sequence conflicti56 – 561Y → S in BAA00645 (PubMed:2020545).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00005 Unassigned DNA. Translation: AAC43398.1.
U14003 Genomic DNA. Translation: AAA97069.1.
U00096 Genomic DNA. Translation: AAC77130.1.
AP009048 Genomic DNA. Translation: BAE78174.1.
D00743 Genomic DNA. Translation: BAA00645.1. Frameshift.
PIRiS56398.
RefSeqiNP_418594.1. NC_000913.3.
WP_000460362.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77130; AAC77130; b4173.
BAE78174; BAE78174; BAE78174.
GeneIDi948688.
KEGGiecj:JW4131.
eco:b4173.
PATRICi32123919. VBIEscCol129921_4304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00005 Unassigned DNA. Translation: AAC43398.1.
U14003 Genomic DNA. Translation: AAA97069.1.
U00096 Genomic DNA. Translation: AAC77130.1.
AP009048 Genomic DNA. Translation: BAE78174.1.
D00743 Genomic DNA. Translation: BAA00645.1. Frameshift.
PIRiS56398.
RefSeqiNP_418594.1. NC_000913.3.
WP_000460362.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ADYelectron microscopy4.5061-426[»]
ProteinModelPortaliP25519.
SMRiP25519. Positions 50-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261252. 360 interactions.
DIPiDIP-9895N.
IntActiP25519. 1 interaction.
STRINGi511145.b4173.

Proteomic databases

PaxDbiP25519.
PRIDEiP25519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77130; AAC77130; b4173.
BAE78174; BAE78174; BAE78174.
GeneIDi948688.
KEGGiecj:JW4131.
eco:b4173.
PATRICi32123919. VBIEscCol129921_4304.

Organism-specific databases

EchoBASEiEB0432.
EcoGeneiEG10437. hflX.

Phylogenomic databases

eggNOGiENOG4105C1N. Bacteria.
COG2262. LUCA.
HOGENOMiHOG000260368.
InParanoidiP25519.
KOiK03665.
OMAiAVLVHIN.
OrthoDBiEOG60SCM2.
PhylomeDBiP25519.

Enzyme and pathway databases

BioCyciEcoCyc:EG10437-MONOMER.
ECOL316407:JW4131-MONOMER.
MetaCyc:EG10437-MONOMER.

Miscellaneous databases

PROiP25519.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00900. GTPase_HflX.
InterProiIPR009022. EFG_III-V.
IPR030394. G_HFLX_dom.
IPR032305. GTP-bd_M.
IPR006073. GTP_binding_domain.
IPR016496. GTPase_HflX.
IPR025121. GTPase_HflX_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10229. PTHR10229. 1 hit.
PfamiPF16360. GTP-bdg_M. 1 hit.
PF13167. GTP-bdg_N. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF006809. GTP-binding_hflX_prd. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 1 hit.
TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
PROSITEiPS51705. G_HFLX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain."
    Noble J.A., Innis M.A., Koonin E.V., Rudd K.E., Banuett F., Herskowitz I.
    Proc. Natl. Acad. Sci. U.S.A. 90:10866-10870(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [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. "Identification and sequence determination of the host factor gene for bacteriophage Q beta."
    Kajitani M., Ishihama A.
    Nucleic Acids Res. 19:1063-1066(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
  6. "Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage lambda."
    Banuett F., Herskowitz I.
    J. Bacteriol. 169:4076-4085(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY FUNCTION.
  7. "E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides."
    Jain N., Dhimole N., Khan A.R., De D., Tomar S.K., Sajish M., Dutta D., Parrack P., Prakash B.
    Biochem. Biophys. Res. Commun. 379:201-205(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT, INTERACTION WITH 50S SUBUNIT, DOMAIN.
  8. "Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach."
    Shields M.J., Fischer J.J., Wieden H.J.
    Biochemistry 48:10793-10802(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  9. "Properties of HflX, an enigmatic protein from Escherichia coli."
    Dutta D., Bandyopadhyay K., Datta A.B., Sardesai A.A., Parrack P.
    J. Bacteriol. 191:2307-2314(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A GTPASE, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.

Entry informationi

Entry nameiHFLX_ECOLI
AccessioniPrimary (citable) accession number: P25519
Secondary accession number(s): Q2M6D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1994
Last modified: April 13, 2016
This is version 128 of the entry and version 3 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.