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Protein

GTPase Era

Gene

era

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity).By similarity
The Era binding site on the 30S subunit overlaps that of protein S1 and is in direct contact with 5 nucleotides directly upstream of the anti-Shine-Dalgarno sequence; the presence of Era may prevent mRNA recruitment. 30S subunits bound to Era are not able to bind to the 50S subunit to make functional ribosomes. Era may serve a role in the final stages of 30S ribosomal subunit assembly.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 21GTPSequence analysis8
Nucleotide bindingi61 – 65GTPSequence analysis5
Nucleotide bindingi125 – 128GTPSequence analysis4

GO - Molecular functioni

  • GTPase activity Source: UniProtKB-HAMAP
  • GTP binding Source: UniProtKB-HAMAP
  • ribosomal small subunit binding Source: UniProtKB
  • small ribosomal subunit rRNA binding Source: UniProtKB

GO - Biological processi

  • ribosomal small subunit assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase Era
Gene namesi
Name:era
Ordered Locus Names:TTHA0120
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004039721 – 301GTPase EraAdd BLAST301

Proteomic databases

PRIDEiQ5SM23.

Interactioni

Subunit structurei

Monomer (Probable). Binds to the 30S ribosomal subunit, between the head and platform, contacting the 16S rRNA. Contacts ribosomal proteins S7 and S18 and may contact proteins S2 and S11.Curated1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0120.

Structurei

Secondary structure

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Helixi20 – 28Combined sources9
Beta strandi37 – 39Combined sources3
Beta strandi46 – 52Combined sources7
Beta strandi55 – 61Combined sources7
Helixi71 – 83Combined sources13
Beta strandi88 – 95Combined sources8
Helixi102 – 111Combined sources10
Helixi112 – 114Combined sources3
Turni115 – 117Combined sources3
Beta strandi120 – 125Combined sources6
Helixi127 – 129Combined sources3
Helixi133 – 142Combined sources10
Beta strandi147 – 151Combined sources5
Helixi157 – 168Combined sources12
Beta strandi184 – 187Combined sources4
Helixi189 – 203Combined sources15
Helixi209 – 212Combined sources4
Beta strandi214 – 223Combined sources10
Turni224 – 226Combined sources3
Beta strandi227 – 238Combined sources12
Helixi239 – 246Combined sources8
Helixi248 – 250Combined sources3
Helixi251 – 268Combined sources18
Beta strandi270 – 280Combined sources11
Helixi284 – 286Combined sources3
Helixi288 – 294Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WF3X-ray1.88A1-301[»]
1X18electron microscopy13.50X1-301[»]
1X1Lelectron microscopy13.50X1-301[»]
ProteinModelPortaliQ5SM23.
SMRiQ5SM23.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SM23.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 173Era-type GAdd BLAST168
Domaini205 – 282KH type-2Add BLAST78

Sequence similaritiesi

Contains 1 KH type-2 domain.Curated

Phylogenomic databases

eggNOGiENOG4105CWT. Bacteria.
COG1159. LUCA.
HOGENOMiHOG000245597.
KOiK03595.
OMAiKVAKDWQ.
PhylomeDBiQ5SM23.

Family and domain databases

CDDicd04163. Era. 1 hit.
Gene3Di3.30.300.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00367. GTPase_Era. 1 hit.
InterProiIPR030388. G_ERA_dom.
IPR005662. GTP-bd_Era.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54814. SSF54814. 1 hit.
TIGRFAMsiTIGR00436. era. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51713. G_ERA. 1 hit.
PS50823. KH_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SM23-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKTYSGFV AIVGKPNVGK STLLNNLLGV KVAPISPRPQ TTRKRLRGIL
60 70 80 90 100
TEGRRQIVFV DTPGLHKPMD ALGEFMDQEV YEALADVNAV VWVVDLRHPP
110 120 130 140 150
TPEDELVARA LKPLVGKVPI LLVGNKLDAA KYPEEAMKAY HELLPEAEPR
160 170 180 190 200
MLSALDERQV AELKADLLAL MPEGPFFYPE DYAKSDQTFG EWVAEILREE
210 220 230 240 250
AMKRLWHEVP YAVATKVEEV AERENGVLYI KAILYVERPS QKAIVIGEGG
260 270 280 290 300
RKIKEIGQAT RKQLEALLGK KVYLDLEVKV YPDWRKDPEA LRELGYRSSV

G
Length:301
Mass (Da):33,809
Last modified:December 21, 2004 - v1
Checksum:iE5403580A8D161F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69943.1.
RefSeqiWP_008630929.1. NC_006461.1.
YP_143386.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69943; BAD69943; BAD69943.
GeneIDi3167951.
KEGGittj:TTHA0120.
PATRICi23955177. VBITheThe93045_0118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69943.1.
RefSeqiWP_008630929.1. NC_006461.1.
YP_143386.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WF3X-ray1.88A1-301[»]
1X18electron microscopy13.50X1-301[»]
1X1Lelectron microscopy13.50X1-301[»]
ProteinModelPortaliQ5SM23.
SMRiQ5SM23.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0120.

Proteomic databases

PRIDEiQ5SM23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD69943; BAD69943; BAD69943.
GeneIDi3167951.
KEGGittj:TTHA0120.
PATRICi23955177. VBITheThe93045_0118.

Phylogenomic databases

eggNOGiENOG4105CWT. Bacteria.
COG1159. LUCA.
HOGENOMiHOG000245597.
KOiK03595.
OMAiKVAKDWQ.
PhylomeDBiQ5SM23.

Miscellaneous databases

EvolutionaryTraceiQ5SM23.

Family and domain databases

CDDicd04163. Era. 1 hit.
Gene3Di3.30.300.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00367. GTPase_Era. 1 hit.
InterProiIPR030388. G_ERA_dom.
IPR005662. GTP-bd_Era.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54814. SSF54814. 1 hit.
TIGRFAMsiTIGR00436. era. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51713. G_ERA. 1 hit.
PS50823. KH_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERA_THET8
AccessioniPrimary (citable) accession number: Q5SM23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 95 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.