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Protein

Glycogen accumulation regulator GarA

Gene

garA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in regulation of glutamate metabolism. Acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB.3 Publications

Enzyme regulationi

Phosphorylation triggers an intra-molecular protein closure, which blocks the FHA binding site and interaction with target enzymes, and switches off the regulatory function of GarA.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • negative regulation of glycolytic process Source: MTBBASE
  • protein autophosphorylation Source: MTBBASE
  • regulation of cellular respiration Source: MTBBASE
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen accumulation regulator GarA
Gene namesi
Name:garA
Ordered Locus Names:Rv1827
ORF Names:MTCY1A11.16c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1827.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211T → A: Lack of phosphorylation by PknG. 1 Publication
Mutagenesisi22 – 221T → A: Does not affect phosphorylation by PknG. 1 Publication
Mutagenesisi95 – 951S → A: Decreases ability to bind to and regulate the activities of Gdh and GltB, but does not affect ability to inhibit Kgd. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 162161Glycogen accumulation regulator GarAPRO_0000103902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei21 – 211Phosphothreonine; by PknG1 Publication
Modified residuei22 – 221Phosphothreonine; by PknB1 Publication

Post-translational modificationi

Phosphorylated on Thr-22 by PknB. Phosphorylated on Thr-21 by PknG. Phosphorylation at either Thr-21 or Thr-22 prevents binding to target enzymes. Phosphorylation at these two threonines is mutually exclusive in vitro. Could also be phosphorylated by PknD, PknE and PknF.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP9WJA9.

PTM databases

iPTMnetiP9WJA9.

Interactioni

Subunit structurei

Monomer. Binds via its FHA domain to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-6405522,EBI-6405522
gdhO532035EBI-6405522,EBI-6405569
kgdP9WIS54EBI-6405522,EBI-6405560
pknBP9WI812EBI-6405522,EBI-2946037
pknGP9WI734EBI-6405522,EBI-6405537

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiP9WJA9. 6 interactions.
STRINGi83332.Rv1827.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Turni27 – 304Combined sources
Beta strandi47 – 504Combined sources
Beta strandi57 – 637Combined sources
Beta strandi69 – 713Combined sources
Beta strandi74 – 818Combined sources
Beta strandi83 – 897Combined sources
Turni90 – 923Combined sources
Beta strandi93 – 964Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi142 – 1476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KFUNMR-A2-162[»]
ProteinModelPortaliP9WJA9.
SMRiP9WJA9. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 12650FHAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108UW8. Bacteria.
COG1716. LUCA.
OMAiFRLVFLN.
PhylomeDBiP9WJA9.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WJA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDMNPDIEK DQTSDEVTVE TTSVFRADFL SELDAPAQAG TESAVSGVEG
60 70 80 90 100
LPPGSALLVV KRGPNAGSRF LLDQAITSAG RHPDSDIFLD DVTVSRRHAE
110 120 130 140 150
FRLENNEFNV VDVGSLNGTY VNREPVDSAV LANGDEVQIG KFRLVFLTGP
160
KQGEDDGSTG GP
Length:162
Mass (Da):17,251
Last modified:April 16, 2014 - v1
Checksum:i18B1C42151ED0CCA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ885576 Genomic DNA. Translation: AFK73561.1.
AL123456 Genomic DNA. Translation: CCP44593.1.
PIRiD70721.
RefSeqiNP_216343.1. NC_000962.3.
WP_003899041.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44593; CCP44593; Rv1827.
GeneIDi885735.
KEGGimtu:Rv1827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ885576 Genomic DNA. Translation: AFK73561.1.
AL123456 Genomic DNA. Translation: CCP44593.1.
PIRiD70721.
RefSeqiNP_216343.1. NC_000962.3.
WP_003899041.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KFUNMR-A2-162[»]
ProteinModelPortaliP9WJA9.
SMRiP9WJA9. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WJA9. 6 interactions.
STRINGi83332.Rv1827.

PTM databases

iPTMnetiP9WJA9.

Proteomic databases

PaxDbiP9WJA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44593; CCP44593; Rv1827.
GeneIDi885735.
KEGGimtu:Rv1827.

Organism-specific databases

TubercuListiRv1827.

Phylogenomic databases

eggNOGiENOG4108UW8. Bacteria.
COG1716. LUCA.
OMAiFRLVFLN.
PhylomeDBiP9WJA9.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete Rv1827 gene sequence of Mycobactarium tuberculosis strain AIIMS/LM/SS/TB-2016 I/05 SP."
    Singh A., Singh S.
    Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: AIIMS/LM/SS/TB-2016 I/05 SP.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  3. "Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions."
    Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C., Alzari P.M.
    J. Mol. Biol. 350:953-963(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-28, INTERACTION WITH PKNB, PHOSPHORYLATION AT THR-22, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.
  4. Cited for: FUNCTION, INTERACTION WITH KGD; GDH AND PKNG, PHOSPHORYLATION AT THR-21, MUTAGENESIS OF THR-21 AND THR-22.
    Strain: ATCC 25618 / H37Rv.
  5. "The FHA-containing protein GarA acts as a phosphorylation-dependent molecular switch in mycobacterial signaling."
    England P., Wehenkel A., Martins S., Hoos S., Andre-Leroux G., Villarino A., Alzari P.M.
    FEBS Lett. 583:301-307(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT.
  6. "Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host."
    Tiwari D., Singh R.K., Goswami K., Verma S.K., Prakash B., Nandicoori V.K.
    J. Biol. Chem. 284:27467-27479(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKNG.
    Strain: ATCC 25618 / H37Rv.
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  8. "An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis."
    Nott T.J., Kelly G., Stach L., Li J., Westcott S., Patel D., Hunt D.M., Howell S., Buxton R.S., O'Hare H.M., Smerdon S.J.
    Sci. Signal. 2:RA12-RA12(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-162, FUNCTION, ENZYME REGULATION, INTERACTION WITH KGD; GDH AND GLTB, MUTAGENESIS OF SER-95.
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiGARA_MYCTU
AccessioniPrimary (citable) accession number: P9WJA9
Secondary accession number(s): I3V6A5, P64897, Q50606
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: January 20, 2016
This is version 18 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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.