GARA_MYCS2
ID GARA_MYCS2 Reviewed; 158 AA.
AC A0QYG2; I7GBT9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Glycogen accumulation regulator GarA;
GN Name=garA; OrderedLocusNames=MSMEG_3647, MSMEI_3561;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, INTERACTION WITH KGD; GDH AND PKNG, AND PHOSPHORYLATION AT
RP THR-20.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL Mol. Microbiol. 70:1408-1423(2008).
CC -!- FUNCTION: Involved in regulation of glutamate metabolism. Acts as a
CC phosphorylation-dependent molecular switch that modulates the
CC activities of Kgd and Gdh. {ECO:0000269|PubMed:19019160}.
CC -!- SUBUNIT: Monomer (By similarity). Binds via its FHA domain to Kgd, Gdh,
CC and the N-terminal region of PknG. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Thr-21 by PknB (By similarity). Phosphorylated
CC on Thr-20 by PknG. Phosphorylation at either Thr-20 or Thr-21 prevents
CC binding to target enzymes. {ECO:0000250, ECO:0000269|PubMed:19019160}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK73997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK73997.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP40024.1; -; Genomic_DNA.
DR RefSeq; WP_014877774.1; NZ_SIJM01000008.1.
DR RefSeq; YP_887950.1; NC_008596.1.
DR PDB; 6I2Q; X-ray; 2.15 A; B=45-158.
DR PDB; 6I2R; X-ray; 2.20 A; B/D=45-158.
DR PDB; 6I2S; X-ray; 2.40 A; B=45-158.
DR PDBsum; 6I2Q; -.
DR PDBsum; 6I2R; -.
DR PDBsum; 6I2S; -.
DR AlphaFoldDB; A0QYG2; -.
DR SMR; A0QYG2; -.
DR IntAct; A0QYG2; 3.
DR STRING; 246196.MSMEI_3561; -.
DR iPTMnet; A0QYG2; -.
DR EnsemblBacteria; ABK73997; ABK73997; MSMEG_3647.
DR EnsemblBacteria; AFP40024; AFP40024; MSMEI_3561.
DR GeneID; 66735030; -.
DR KEGG; msg:MSMEI_3561; -.
DR KEGG; msm:MSMEG_3647; -.
DR PATRIC; fig|246196.19.peg.3595; -.
DR eggNOG; COG1716; Bacteria.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..158
FT /note="Glycogen accumulation regulator GarA"
FT /id="PRO_0000419534"
FT DOMAIN 76..125
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT MOD_RES 20
FT /note="Phosphothreonine; by PknG"
FT /evidence="ECO:0000269|PubMed:19019160"
FT MOD_RES 21
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000250"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6I2Q"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:6I2Q"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6I2Q"
SQ SEQUENCE 158 AA; 16584 MW; 884B68B7C37084BE CRC64;
MTDKDSNLGA DQSEDVTVET TSVFRADFLN ELDAPAAAGT EGAVSGVEGL PSGSALLVVK
RGPNAGSRFL LDQPTTSAGR HPDSDIFLDD VTVSRRHAEF RLEGGEFQVV DVGSLNGTYV
NREPVDSAVL ANGDEVQIGK FRLVFLTGPK SDDSGSNA
