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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...

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6022-MONOMER.

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)DescriptionActionsGraphical viewLength
Mutagenesisi21T → A: Lack of phosphorylation by PknG. 1 Publication1
Mutagenesisi22T → A: Does not affect phosphorylation by PknG. 1 Publication1
Mutagenesisi95S → A: Decreases ability to bind to and regulate the activities of Gdh and GltB, but does not affect ability to inhibit Kgd. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001039022 – 162Glycogen accumulation regulator GarAAdd BLAST161

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei21Phosphothreonine; by PknG1 Publication1
Modified residuei22Phosphothreonine; by PknB1 Publication1

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 interactors.
STRINGi83332.Rv1827.

Structurei

Secondary structure

1162
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Turni27 – 30Combined sources4
Beta strandi47 – 50Combined sources4
Beta strandi57 – 63Combined sources7
Beta strandi69 – 71Combined sources3
Beta strandi74 – 81Combined sources8
Beta strandi83 – 89Combined sources7
Turni90 – 92Combined sources3
Beta strandi93 – 96Combined sources4
Beta strandi98 – 104Combined sources7
Beta strandi107 – 111Combined sources5
Beta strandi119 – 121Combined sources3
Beta strandi127 – 130Combined sources4
Beta strandi136 – 139Combined sources4
Beta strandi142 – 147Combined sources6

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 126FHAPROSITE-ProRule annotationAdd BLAST50

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108UW8. Bacteria.
COG1716. LUCA.
OMAiNREPVDT.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KFUNMR-A2-162[»]
ProteinModelPortaliP9WJA9.
SMRiP9WJA9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WJA9. 6 interactors.
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.
OMAiNREPVDT.
PhylomeDBiP9WJA9.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6022-MONOMER.

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...

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: November 2, 2016
This is version 21 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.