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Database: UniProt
Entry: Q8F063_LEPIN
LinkDB: Q8F063_LEPIN
Original site: Q8F063_LEPIN 
ID   Q8F063_LEPIN            Unreviewed;       518 AA.
AC   Q8F063;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900};
DE   AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN   Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900,
GN   ECO:0000313|EMBL:AAN50832.1};
GN   OrderedLocusNames=LA_3634 {ECO:0000313|EMBL:AAN50832.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN50832.1, ECO:0000313|Proteomes:UP000001408};
RN   [1] {ECO:0000313|EMBL:AAN50832.1, ECO:0000313|Proteomes:UP000001408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 {ECO:0000313|EMBL:AAN50832.1,
RC   ECO:0000313|Proteomes:UP000001408};
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA   Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA   Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA   Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA   Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA   Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC       have a role during protein synthesis or ribosome biogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}.
CC       Note=May associate with membranes. {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. HflX GTPase family. {ECO:0000256|HAMAP-Rule:MF_00900}.
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DR   EMBL; AE010300; AAN50832.1; -; Genomic_DNA.
DR   RefSeq; NP_713814.1; NC_004342.2.
DR   AlphaFoldDB; Q8F063; -.
DR   STRING; 189518.LA_3634; -.
DR   PaxDb; 189518-LA_3634; -.
DR   EnsemblBacteria; AAN50832; AAN50832; LA_3634.
DR   KEGG; lil:LA_3634; -.
DR   PATRIC; fig|189518.3.peg.3609; -.
DR   HOGENOM; CLU_019597_7_1_12; -.
DR   InParanoid; Q8F063; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000001408; Chromosome I.
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; 6.10.250.2860; -; 1.
DR   Gene3D; 3.40.50.11060; GTPase HflX, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03156; GTP_HflX; 1.
DR   PANTHER; PTHR10229:SF0; GTP-BINDING PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10229; GTP-BINDING PROTEIN HFLX; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00900}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000001408}.
FT   DOMAIN          315..507
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   COILED          281..308
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   518 AA;  58962 MW;  0EA9439A27F1CC25 CRC64;
     MLVGSDNSIE IPFLDRLRIS EARLRGLRLV HTHLKGEPLN QEDLTDLALL RLDYFTAIVM
     DHFGNPNGYY SAHLNPESED ELWTVLPKQY PGQLTEGILE EILEIESRLS RSKKNLKDAQ
     KENRAFLVGV YPERNVGRHP SLSMEELKEL CKTAEVHVVD TFIQRKNRLD PSTVLGKGKL
     EEIILKAIQK HVELLVFDLE LTPSQAKKIS DIADIKVIDR TQLILDIFAR NAKSRDGKLQ
     VELAQLKYLK GRLTELDDNM SRLTGGIGGR GPGETKLEIG KRRVEERITR LEVELKSLKK
     RREINRRQRK KNELPAVGIV GYTNAGKSTF LNALTNSEVL SENKLFATLD PTTRRIRFPE
     EREIIISDTV GFIHDLPPEL SNAFKATLEE LGDSDLLVHV VDVSNPDYKL QMEAVEKILE
     ELELSHIPMI QVFNKIDRLE KFKIWVIENG YKKSSSVNHG PGLEAITDLK EELGIDTFSD
     SILVSAFQGW GLKTFLDLLE DRIYNLSRSN YSNTSSVY
//
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