HFLX_SACS2
ID HFLX_SACS2 Reviewed; 356 AA.
AC Q980M3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900};
DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900};
GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=SSO0269;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH 50S SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=21478358; DOI=10.1128/jb.01552-10;
RA Blombach F., Launay H., Zorraquino V., Swarts D.C., Cabrita L.D.,
RA Benelli D., Christodoulou J., Londei P., van der Oost J.;
RT "An HflX-Type GTPase from Sulfolobus solfataricus binds to the 50S
RT ribosomal subunit in all nucleotide-bound states.";
RL J. Bacteriol. 193:2861-2867(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH GDP AND
RP OF MUTANTS PRO-235 AND SER-235, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASN-189; THR-193; THR-213; GLY-235 AND PHE-236.
RX PubMed=20400571; DOI=10.1093/jb/mvq039;
RA Huang B., Wu H., Hao N., Blombach F., van der Oost J., Li X., Zhang X.C.,
RA Rao Z.;
RT "Functional study on GTP hydrolysis by the GTP-binding protein from
RT Sulfolobus solfataricus, a member of the HflX family.";
RL J. Biochem. 148:103-113(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION AS A
RP GTPASE, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=19787775; DOI=10.1002/prot.22599;
RA Wu H., Sun L., Blombach F., Brouns S.J., Snijders A.P., Lorenzen K.,
RA van den Heuvel R.H., Heck A.J., Fu S., Li X., Zhang X.C., Rao Z.,
RA van der Oost J.;
RT "Structure of the ribosome associating GTPase HflX.";
RL Proteins 78:705-713(2010).
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis. Specific
CC for GTP. {ECO:0000255|HAMAP-Rule:MF_00900, ECO:0000269|PubMed:19787775,
CC ECO:0000269|PubMed:21478358}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC -!- ACTIVITY REGULATION: GTPase activity is stimulated by the presence of
CC 50S ribosomal subunits. Hydrolysis is probably regulated by the HflX N-
CC terminal domain. {ECO:0000269|PubMed:19787775,
CC ECO:0000269|PubMed:21478358}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 uM for GTP {ECO:0000269|PubMed:20400571};
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. Does not
CC associate with 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:19787775, ECO:0000269|PubMed:20400571,
CC ECO:0000269|PubMed:21478358}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}.
CC Note=May associate with membranes. {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP-Rule:MF_00900}.
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DR EMBL; AE006641; AAK40607.1; -; Genomic_DNA.
DR PIR; H90168; H90168.
DR RefSeq; WP_009990543.1; NC_002754.1.
DR PDB; 2QTF; X-ray; 2.00 A; A=1-356.
DR PDB; 2QTH; X-ray; 2.00 A; A=1-356.
DR PDB; 3KXI; X-ray; 2.65 A; A=1-356.
DR PDB; 3KXK; X-ray; 2.35 A; A/B=1-356.
DR PDB; 3KXL; X-ray; 2.50 A; A/B=1-356.
DR PDBsum; 2QTF; -.
DR PDBsum; 2QTH; -.
DR PDBsum; 3KXI; -.
DR PDBsum; 3KXK; -.
DR PDBsum; 3KXL; -.
DR AlphaFoldDB; Q980M3; -.
DR SMR; Q980M3; -.
DR STRING; 273057.SSO0269; -.
DR EnsemblBacteria; AAK40607; AAK40607; SSO0269.
DR GeneID; 44129241; -.
DR KEGG; sso:SSO0269; -.
DR PATRIC; fig|273057.12.peg.263; -.
DR eggNOG; arCOG00353; Archaea.
DR HOGENOM; CLU_019597_2_0_2; -.
DR InParanoid; Q980M3; -.
DR OMA; AEMKTGR; -.
DR PhylomeDB; Q980M3; -.
DR BRENDA; 3.6.5.3; 6163.
DR EvolutionaryTrace; Q980M3; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR CDD; cd01878; HflX; 1.
DR Gene3D; 3.40.50.11060; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00900; GTPase_HflX; 1.
DR InterPro; IPR030394; G_HFLX_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR032305; GTP-bd_M.
DR InterPro; IPR016496; GTPase_HflX.
DR InterPro; IPR025121; GTPase_HflX_N.
DR InterPro; IPR042108; GTPase_HflX_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR10229; PTHR10229; 1.
DR Pfam; PF16360; GTP-bdg_M; 1.
DR Pfam; PF13167; GTP-bdg_N; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..356
FT /note="GTPase HflX"
FT /id="PRO_0000412528"
FT DOMAIN 180..356
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 186..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900,
FT ECO:0000305|PubMed:19787775, ECO:0000305|PubMed:20400571"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 211..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 232..235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900,
FT ECO:0000305|PubMed:19787775, ECO:0000305|PubMed:20400571"
FT BINDING 334..336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900,
FT ECO:0000305|PubMed:19787775, ECO:0000305|PubMed:20400571"
FT MUTAGEN 189
FT /note="N->P: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT MUTAGEN 193
FT /note="T->N: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT MUTAGEN 213
FT /note="T->V: Decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT MUTAGEN 235
FT /note="G->P: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT MUTAGEN 235
FT /note="G->S: Decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT MUTAGEN 236
FT /note="F->P: Increase in KM for GTP and in GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:20400571"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2QTF"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2QTF"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 145..164
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2QTF"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3KXK"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:2QTF"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:2QTF"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:2QTF"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:2QTF"
SQ SEQUENCE 356 AA; 40538 MW; 602D4DBBE3BEAB1C CRC64;
MKTAALFVSK EFEEEAIALV EGANYKVTSI YKLPKSPNVK FYIQYDKLQQ IKNDEEISTL
IIFEQLKPRH FINIRRELKG KEVLDKILLL LEIFALHAGS KEAKMQIELA RLKYELPIIK
ETYTKSKIGE QQGPLGAGTY GVESTIKFYK RRINKLMKEL ESIKIFKEKS IESNKRNNIP
SIGIVGYTNS GKTSLFNSLT GLTQKVDTKL FTTMSPKRYA IPINNRKIML VDTVGFIRGI
PPQIVDAFFV TLSEAKYSDA LILVIDSTFS ENLLIETLQS SFEILREIGV SGKPILVTLN
KIDKINGDLY KKLDLVEKLS KELYSPIFDV IPISALKRTN LELLRDKIYQ LATQLS
