HFLX_ECOLI
ID HFLX_ECOLI Reviewed; 426 AA.
AC P25519; Q2M6D2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 3.
DT 03-AUG-2022, entry version 159.
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};
GN OrderedLocusNames=b4173, JW4131;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8248183; DOI=10.1073/pnas.90.22.10866;
RA Noble J.A., Innis M.A., Koonin E.V., Rudd K.E., Banuett F., Herskowitz I.;
RT "The Escherichia coli hflA locus encodes a putative GTP-binding protein and
RT two membrane proteins, one of which contains a protease-like domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10866-10870(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=2020545; DOI=10.1093/nar/19.5.1063;
RA Kajitani M., Ishihama A.;
RT "Identification and sequence determination of the host factor gene for
RT bacteriophage Q beta.";
RL Nucleic Acids Res. 19:1063-1066(1991).
RN [6]
RP PRELIMINARY FUNCTION.
RX PubMed=3040675; DOI=10.1128/jb.169.9.4076-4085.1987;
RA Banuett F., Herskowitz I.;
RT "Identification of polypeptides encoded by an Escherichia coli locus (hflA)
RT that governs the lysis-lysogeny decision of bacteriophage lambda.";
RL J. Bacteriol. 169:4076-4085(1987).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH 50S SUBUNIT, AND
RP DOMAIN.
RX PubMed=19109926; DOI=10.1016/j.bbrc.2008.12.072;
RA Jain N., Dhimole N., Khan A.R., De D., Tomar S.K., Sajish M., Dutta D.,
RA Parrack P., Prakash B.;
RT "E. coli HflX interacts with 50S ribosomal subunits in presence of
RT nucleotides.";
RL Biochem. Biophys. Res. Commun. 379:201-205(2009).
RN [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19824612; DOI=10.1021/bi901074h;
RA Shields M.J., Fischer J.J., Wieden H.J.;
RT "Toward understanding the function of the universally conserved GTPase HflX
RT from Escherichia coli: a kinetic approach.";
RL Biochemistry 48:10793-10802(2009).
RN [9]
RP FUNCTION AS A GTPASE, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=19181811; DOI=10.1128/jb.01353-08;
RA Dutta D., Bandyopadhyay K., Datta A.B., Sardesai A.A., Parrack P.;
RT "Properties of HflX, an enigmatic protein from Escherichia coli.";
RL J. Bacteriol. 191:2307-2314(2009).
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis. In vitro,
CC also exhibits ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811,
CC ECO:0000269|PubMed:19824612}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC -!- ACTIVITY REGULATION: Intrinsic GTPase activity is very slow and can be
CC stimulated by the presence of 50S ribosomal subunits or 70S ribosomes.
CC GTPase activity is inhibited by ATP. {ECO:0000269|PubMed:19109926,
CC ECO:0000269|PubMed:19181811, ECO:0000269|PubMed:19824612}.
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. This
CC interaction occurs in the presence of GTP, GDP, ATP or ADP, but not in
CC their absence. {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:19181811}. Note=May associate with membranes.
CC -!- DOMAIN: Full-length protein is required for specific association with
CC the 50S ribosomal subunit. {ECO:0000269|PubMed:19109926}.
CC -!- DISRUPTION PHENOTYPE: Disruption does not affect lambda lysogeny or the
CC transposition frequency of transposable elements.
CC {ECO:0000269|PubMed:19181811}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00645.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00005; AAC43398.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97069.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77130.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78174.1; -; Genomic_DNA.
DR EMBL; D00743; BAA00645.1; ALT_FRAME; Genomic_DNA.
DR PIR; S56398; S56398.
DR RefSeq; NP_418594.1; NC_000913.3.
DR RefSeq; WP_000460362.1; NZ_LN832404.1.
DR PDB; 5ADY; EM; 4.50 A; 6=1-426.
DR PDB; 5ZZM; EM; 8.10 A; A=1-426.
DR PDBsum; 5ADY; -.
DR PDBsum; 5ZZM; -.
DR AlphaFoldDB; P25519; -.
DR SMR; P25519; -.
DR BioGRID; 4261252; 369.
DR BioGRID; 852980; 1.
DR DIP; DIP-9895N; -.
DR IntAct; P25519; 1.
DR STRING; 511145.b4173; -.
DR jPOST; P25519; -.
DR PaxDb; P25519; -.
DR PRIDE; P25519; -.
DR EnsemblBacteria; AAC77130; AAC77130; b4173.
DR EnsemblBacteria; BAE78174; BAE78174; BAE78174.
DR GeneID; 948688; -.
DR KEGG; ecj:JW4131; -.
DR KEGG; eco:b4173; -.
DR PATRIC; fig|1411691.4.peg.2528; -.
DR EchoBASE; EB0432; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_2_1_6; -.
DR InParanoid; P25519; -.
DR OMA; AEMKTGR; -.
DR PhylomeDB; P25519; -.
DR BioCyc; EcoCyc:EG10437-MON; -.
DR BioCyc; MetaCyc:EG10437-MON; -.
DR PRO; PR:P25519; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:EcoCyc.
DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0032790; P:ribosome disassembly; IDA:EcoCyc.
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; IPR035647; EFG_III/V.
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; IPR045498; HflX_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10229; PTHR10229; 1.
DR Pfam; PF16360; GTP-bdg_M; 1.
DR Pfam; PF13167; GTP-bdg_N; 1.
DR Pfam; PF19275; HflX_C; 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 SUPFAM; SSF54980; SSF54980; 1.
DR TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..426
FT /note="GTPase HflX"
FT /id="PRO_0000122463"
FT DOMAIN 198..365
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 204..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 229..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 251..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 317..320
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 343..345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT CONFLICT 53
FT /note="H -> R (in Ref. 5; BAA00645)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="Y -> S (in Ref. 5; BAA00645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48327 MW; 8D0A5BE92EE32591 CRC64;
MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE ALQVITGSRK APHPKYFVGE
GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG
KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLER
VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNRITEA RVYAADQLFA TLDPTLRRID
VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIEAVNT
VLEEIDAHEI PTLLVMNKID MLEDFEPRID RDEENKPNRV WLSAQTGAGI PQLFQALTER
LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA
LIDYLI
