ARGK_ECOLI
ID ARGK_ECOLI Reviewed; 331 AA.
AC P27254; Q2M9S4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=GTPase ArgK {ECO:0000305|PubMed:18950999};
DE EC=3.6.5.- {ECO:0000269|PubMed:18950999};
DE AltName: Full=G-protein chaperone {ECO:0000305};
GN Name=argK; Synonyms=ygfD; OrderedLocusNames=b2918, JW2885;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PRELIMINARY CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=9733684; DOI=10.1128/jb.180.18.4828-4833.1998;
RA Celis R.T.F., Leadlay P.F., Roy I., Hansen A.;
RT "Phosphorylation of the periplasmic binding protein in two transport
RT systems for arginine incorporation in Escherichia coli K-12 is unrelated to
RT the function of the transport system.";
RL J. Bacteriol. 180:4828-4833(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, GTPASE ACTIVITY, SUBUNIT, AND INTERACTION WITH SCPA.
RX PubMed=18950999; DOI=10.1016/j.micres.2008.08.006;
RA Froese D.S., Dobson C.M., White A.P., Wu X., Padovani D., Banerjee R.,
RA Haller T., Gerlt J.A., Surette M.G., Gravel R.A.;
RT "Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in
RT Escherichia coli.";
RL Microbiol. Res. 164:1-8(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of LAO/AO transport system kinase.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Binds and hydrolyzes GTP (PubMed:18950999). Likely functions
CC as a G-protein chaperone that assists AdoCbl cofactor delivery to the
CC methylmalonyl-CoA mutase (MCM) ScpA and reactivation of the enzyme
CC during catalysis. {ECO:0000269|PubMed:18950999, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:18950999};
CC -!- SUBUNIT: Monomer. Interacts with the methylmalonyl-CoA mutase ScpA.
CC {ECO:0000269|PubMed:18950999}.
CC -!- MISCELLANEOUS: Part of an operon that encodes enzymes converting
CC succinate to propionate. {ECO:0000305|PubMed:18950999}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a membrane protein kinase
CC involved in phosphorylation of the AO and LAO periplasmic-binding
CC proteins (PubMed:9733684). However, its role needs to be reexamined.
CC {ECO:0000305|PubMed:9733684}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47312.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X66836; CAA47312.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U28377; AAA69085.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75955.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76982.1; -; Genomic_DNA.
DR PIR; E65076; E65076.
DR RefSeq; NP_417393.1; NC_000913.3.
DR RefSeq; WP_000606525.1; NZ_SSZK01000003.1.
DR PDB; 2P67; X-ray; 1.80 A; A=2-331.
DR PDBsum; 2P67; -.
DR AlphaFoldDB; P27254; -.
DR SMR; P27254; -.
DR BioGRID; 4259325; 18.
DR BioGRID; 851733; 8.
DR IntAct; P27254; 13.
DR STRING; 511145.b2918; -.
DR PaxDb; P27254; -.
DR PRIDE; P27254; -.
DR EnsemblBacteria; AAC75955; AAC75955; b2918.
DR EnsemblBacteria; BAE76982; BAE76982; BAE76982.
DR GeneID; 947412; -.
DR KEGG; ecj:JW2885; -.
DR KEGG; eco:b2918; -.
DR PATRIC; fig|1411691.4.peg.3814; -.
DR EchoBASE; EB1415; -.
DR eggNOG; COG1703; Bacteria.
DR HOGENOM; CLU_043725_2_2_6; -.
DR InParanoid; P27254; -.
DR OMA; WMWERID; -.
DR PhylomeDB; P27254; -.
DR BioCyc; EcoCyc:EG11445-MON; -.
DR BioCyc; MetaCyc:EG11445-MON; -.
DR EvolutionaryTrace; P27254; -.
DR PRO; PR:P27254; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005129; GTPase_ArgK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23408; PTHR23408; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00750; lao; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..331
FT /note="GTPase ArgK"
FT /id="PRO_0000157816"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 68
FT /note="S -> R (in strain: RC101)"
FT VARIANT 154
FT /note="T -> A (in strain: RC101)"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2P67"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:2P67"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2P67"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 265..292
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:2P67"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:2P67"
SQ SEQUENCE 331 AA; 36704 MW; 02C27AD2000C6137 CRC64;
MINEATLAES IRRLRQGERA TLAQAMTLVE SRHPRHQALS TQLLDAIMPY CGNTLRLGVT
GTPGAGKSTF LEAFGMLLIR EGLKVAVIAV DPSSPVTGGS ILGDKTRMND LARAEAAFIR
PVPSSGHLGG ASQRARELML LCEAAGYDVV IVETVGVGQS ETEVARMVDC FISLQIAGGG
DDLQGIKKGL MEVADLIVIN KDDGDNHTNV AIARHMYESA LHILRRKYDE WQPRVLTCSA
LEKRGIDEIW HAIIDFKTAL TASGRLQQVR QQQSVEWLRK QTEEEVLNHL FANEDFDRYY
RQTLLAVKNN TLSPRTGLRQ LSEFIQTQYF D
