HFLX_LEPBJ
ID HFLX_LEPBJ Reviewed; 462 AA.
AC Q04PB3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 90.
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=LBJ_2854;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00900}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ77257.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000350; ABJ77257.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q04PB3; -.
DR SMR; Q04PB3; -.
DR PRIDE; Q04PB3; -.
DR EnsemblBacteria; ABJ77257; ABJ77257; LBJ_2854.
DR KEGG; lbj:LBJ_2854; -.
DR HOGENOM; CLU_019597_7_1_12; -.
DR Proteomes; UP000000656; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding.
FT CHAIN 1..462
FT /note="GTPase HflX"
FT /id="PRO_0000412660"
FT DOMAIN 255..452
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 261..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 286..290
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 308..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 374..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 430..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ SEQUENCE 462 AA; 52425 MW; 3DE73ED0109DD597 CRC64;
MDTSGNPNGY YSAHLNPESD DLWSVLPKKY PGQLTEGILE EILEIESRLS RSKKNLKDAQ
KENRAFLVGV YPERSVGRHP SLSMEELKEL CRTAEVHVVD TFIQRKNRLD PSTVLGKGKL
EEIILKAIQK HVELLVFDLE LTPSQAKKIS DIADIKVIDR TQLILDIFAR NAKSRDGKLQ
VELAQLKYLK GRLTELDDNM SRLTGGIGGR GPGETKLEIG KRRVEERITR LEVELKSLKK
RREINRRQRK RNELPAVGIV GYTNAGKSTF LNALTNSEIL SENKLFATLD PTTRRIRFPE
EREIIISDTV GFIHDLPPEL SNAFKATLEE LGDSDLLVHV VDVSNPDYKL QMEAVEKILE
ELELSHIPMI QVFNKIDNLE KFKTWKIESD SNGYKTFSHP SINHGPGLEA IADLKEELGI
DVHSDTVLVS AYQGWGLKAF LDLLEEKIYN LPRLNYSIAE KL