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Protein

Transcription elongation factor GreA

Gene

greA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.

GO - Molecular functioni

  • bacterial-type RNA polymerase holo enzyme binding Source: EcoCyc
  • DNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  • DNA-templated transcription, elongation Source: EcoCyc
  • regulation of DNA-templated transcription, elongation Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10415-MONOMER.
ECOL316407:JW3148-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor GreA
Alternative name(s):
Transcript cleavage factor GreA
Gene namesi
Name:greA
Ordered Locus Names:b3181, JW3148
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10415. greA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Transcription elongation factor GreAPRO_0000176921Add
BLAST

Proteomic databases

PaxDbiP0A6W5.
PRIDEiP0A6W5.

2D gel databases

SWISS-2DPAGEP0A6W5.

Interactioni

Protein-protein interaction databases

DIPiDIP-35800N.
IntActiP0A6W5. 51 interactions.
STRINGi511145.b3181.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi8 – 2316Combined sources
Helixi25 – 3713Combined sources
Helixi42 – 443Combined sources
Helixi46 – 7126Combined sources
Beta strandi72 – 754Combined sources
Helixi77 – 793Combined sources
Beta strandi91 – 966Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1088Combined sources
Turni110 – 1123Combined sources
Helixi115 – 1173Combined sources
Beta strandi119 – 1246Combined sources
Helixi125 – 1306Combined sources
Beta strandi150 – 1567Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GRJX-ray2.20A1-158[»]
ProteinModelPortaliP0A6W5.
SMRiP0A6W5. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6W5.

Family & Domainsi

Sequence similaritiesi

Belongs to the GreA/GreB family.Curated

Phylogenomic databases

eggNOGiCOG0782.
HOGENOMiHOG000241145.
InParanoidiP0A6W5.
KOiK03624.
OMAiHNEGRIA.
OrthoDBiEOG686NQ9.
PhylomeDBiP0A6W5.

Family and domain databases

Gene3Di1.10.287.180. 1 hit.
3.10.50.30. 1 hit.
HAMAPiMF_00105. GreA_GreB.
InterProiIPR018151. TF_GreA/GreB_CS.
IPR006359. Tscrpt_elong_fac_GreA.
IPR028624. Tscrpt_elong_fac_GreA/B.
IPR001437. Tscrpt_elong_fac_GreA/B_C.
IPR023459. Tscrpt_elong_fac_GreA/B_fam.
IPR022691. Tscrpt_elong_fac_GreA/B_N.
[Graphical view]
PfamiPF01272. GreA_GreB. 1 hit.
PF03449. GreA_GreB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006092. GreA_GreB. 1 hit.
SUPFAMiSSF46557. SSF46557. 1 hit.
TIGRFAMsiTIGR01462. greA. 1 hit.
PROSITEiPS00829. GREAB_1. 1 hit.
PS00830. GREAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6W5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIPMTLRG AEKLREELDF LKSVRRPEII AAIAEAREHG DLKENAEYHA
60 70 80 90 100
AREQQGFCEG RIKDIEAKLS NAQVIDVTKM PNNGRVIFGA TVTVLNLDSD
110 120 130 140 150
EEQTYRIVGD DEADFKQNLI SVNSPIARGL IGKEEDDVVV IKTPGGEVEF

EVIKVEYL
Length:158
Mass (Da):17,641
Last modified:March 29, 2005 - v1
Checksum:i9E7DFAFE838AC340
GO

Sequence cautioni

The sequence AAA57982.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54718 Genomic DNA. Translation: CAA38521.1.
U01376 Genomic DNA. Translation: AAA97506.1.
U18997 Genomic DNA. Translation: AAA57982.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76213.2.
AP009048 Genomic DNA. Translation: BAE77225.1.
PIRiG65108.
RefSeqiNP_417648.4. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76213; AAC76213; b3181.
BAE77225; BAE77225; BAE77225.
GeneIDi947696.
KEGGiecj:Y75_p3101.
eco:b3181.
PATRICi32121780. VBIEscCol129921_3274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54718 Genomic DNA. Translation: CAA38521.1.
U01376 Genomic DNA. Translation: AAA97506.1.
U18997 Genomic DNA. Translation: AAA57982.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76213.2.
AP009048 Genomic DNA. Translation: BAE77225.1.
PIRiG65108.
RefSeqiNP_417648.4. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GRJX-ray2.20A1-158[»]
ProteinModelPortaliP0A6W5.
SMRiP0A6W5. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35800N.
IntActiP0A6W5. 51 interactions.
STRINGi511145.b3181.

2D gel databases

SWISS-2DPAGEP0A6W5.

Proteomic databases

PaxDbiP0A6W5.
PRIDEiP0A6W5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76213; AAC76213; b3181.
BAE77225; BAE77225; BAE77225.
GeneIDi947696.
KEGGiecj:Y75_p3101.
eco:b3181.
PATRICi32121780. VBIEscCol129921_3274.

Organism-specific databases

EchoBASEiEB0410.
EcoGeneiEG10415. greA.

Phylogenomic databases

eggNOGiCOG0782.
HOGENOMiHOG000241145.
InParanoidiP0A6W5.
KOiK03624.
OMAiHNEGRIA.
OrthoDBiEOG686NQ9.
PhylomeDBiP0A6W5.

Enzyme and pathway databases

BioCyciEcoCyc:EG10415-MONOMER.
ECOL316407:JW3148-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6W5.
PROiP0A6W5.

Family and domain databases

Gene3Di1.10.287.180. 1 hit.
3.10.50.30. 1 hit.
HAMAPiMF_00105. GreA_GreB.
InterProiIPR018151. TF_GreA/GreB_CS.
IPR006359. Tscrpt_elong_fac_GreA.
IPR028624. Tscrpt_elong_fac_GreA/B.
IPR001437. Tscrpt_elong_fac_GreA/B_C.
IPR023459. Tscrpt_elong_fac_GreA/B_fam.
IPR022691. Tscrpt_elong_fac_GreA/B_N.
[Graphical view]
PfamiPF01272. GreA_GreB. 1 hit.
PF03449. GreA_GreB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006092. GreA_GreB. 1 hit.
SUPFAMiSSF46557. SSF46557. 1 hit.
TIGRFAMsiTIGR01462. greA. 1 hit.
PROSITEiPS00829. GREAB_1. 1 hit.
PS00830. GREAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of greA, a suppressor gene that restores growth of an Escherichia coli RNA polymerase mutant at high temperature."
    Sparkowski J., Das A.
    Nucleic Acids Res. 18:6443-6443(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Wang R., Kushner S.R.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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. "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.
  6. "Crystal structure of the GreA transcript cleavage factor from Escherichia coli."
    Stebbins C.E., Borukhov S., Orlova M., Polyakov A., Goldfarb A., Darst S.A.
    Nature 373:636-640(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiGREA_ECOLI
AccessioniPrimary (citable) accession number: P0A6W5
Secondary accession number(s): P21346
, P78111, Q2M931, Q8X9K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 24, 2015
This is version 99 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

External Data

Dasty 3

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 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.