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Database: UniProt
Entry: Q891Y6_CLOTE
LinkDB: Q891Y6_CLOTE
Original site: Q891Y6_CLOTE 
ID   Q891Y6_CLOTE            Unreviewed;       593 AA.
AC   Q891Y6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 133.
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:AAO36709.1};
GN   OrderedLocusNames=CTC_02227 {ECO:0000313|EMBL:AAO36709.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36709.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO36709.1, ECO:0000313|Proteomes:UP000001412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA   Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO36709.1; -; Genomic_DNA.
DR   RefSeq; WP_011100370.1; NC_004557.1.
DR   AlphaFoldDB; Q891Y6; -.
DR   STRING; 212717.CTC_02227; -.
DR   GeneID; 24254473; -.
DR   KEGG; ctc:CTC_02227; -.
DR   HOGENOM; CLU_019597_7_1_9; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000001412; Chromosome.
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; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   3: Inferred from homology;
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:UP000001412}.
FT   DOMAIN          362..539
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
SQ   SEQUENCE   593 AA;  67215 MW;  47406158EAC64946 CRC64;
     MIYGNTNGVR DTVLEKLEEI YIMKIAKDEI CSRELISVLA YFTELIGREI SVAINRRGTV
     ESVTLGDSST VELPILEIKQ KKLSGIRIVH THPSGNSTLS SLDLSALLKL KLDCIVAIGV
     LEGEAKEITV GFCDIENDLL KWDSTKKLSV DEFLSMNILE KLDYIEDIIK GSKVEEDYGE
     KAIIVGIENE ESLEELAELA RACEVSVLGR IFQKRSKMDP ALYIGSGKVS EVGYLAQKTR
     ANVIIFDDEL SGSQLRNLEK YLGIKVIDRT TLILEIFSKR AKSREGKIQV ELAQLKYRLP
     RLIGMGAVLS RTGGGIGTRG PGEQKLETDR RHIKNRIYDL SKELEKIKKI RKTQRASRNE
     VPKVSLVGYT NSGKSTLRNY MYNLFQSKEL SKKDNVLEAD MLFATLDTTT RAIYLPDNRD
     ITLTDTVGFI RKLPHDLVES FKSTLEEVMD ADLLLHVVDI SSIHYLEQIE AVNNVLRELN
     ALNKPSIILI NKIDKINEDE LETKLENLKN YKYVCISAKE GINIDVLLKE IINKLPNKLK
     KAEYLIPYNK QDVVAYLHRN AKVHEENYKD NGTYVRAEVD DLVYNVCNEY MIK
//
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