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Database: UniProt
Entry: A0A381JAK9_9CLOT
LinkDB: A0A381JAK9_9CLOT
Original site: A0A381JAK9_9CLOT 
ID   A0A381JAK9_9CLOT        Unreviewed;       597 AA.
AC   A0A381JAK9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   18-JUN-2025, entry version 23.
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:SUY47412.1};
GN   ORFNames=NCTC9836_01743 {ECO:0000313|EMBL:SUY47412.1};
OS   Clostridium putrefaciens.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=99675 {ECO:0000313|EMBL:SUY47412.1, ECO:0000313|Proteomes:UP000254664};
RN   [1] {ECO:0000313|EMBL:SUY47412.1, ECO:0000313|Proteomes:UP000254664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC9836 {ECO:0000313|EMBL:SUY47412.1,
RC   ECO:0000313|Proteomes:UP000254664};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UFWZ01000001; SUY47412.1; -; Genomic_DNA.
DR   RefSeq; WP_115641371.1; NZ_UFWZ01000001.1.
DR   AlphaFoldDB; A0A381JAK9; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000254664; Unassembled WGS sequence.
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   GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR   CDD; cd01878; HflX; 1.
DR   FunFam; 3.40.50.11060:FF:000001; GTPase 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|ARBA:ARBA00022490, 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:UP000254664}.
FT   DOMAIN          364..542
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
SQ   SEQUENCE   597 AA;  67055 MW;  8345126774C179A1 CRC64;
     MIYGSIEGVK KSIIDSLEDI NEMTLPKYML FTEEILNILV DSSSRLGREI SVAIDRKGKV
     VGVAIGDSST VEIPMINIKE KKLSGVRIIH THPNGNSRLS AIDNSALLKL KLDCIVAIGI
     FNEKLTDISV GFCDVKENLL IPELMEGLTL KESLNFDFMD KVKNIETIIE SNEIDEDNGE
     KAIIVGSDTE ESLDELGQLA KACDIPVLFS VFQNRSKIDP TYYIGKGKVE EVALLRQGLR
     ANVVIFDDEL SGSQVRNLEE VIGCKVIDRT TLILEIFATR AKTKESKIQV ELAQLKYRLS
     RLTGLGTILS RTGGGIGTRG PGEKKLETDR RHIRETVYDL TSELSKIKKT RETQREKRNK
     QNIPQVSLVG YTNSGKSTLR NALYDMAMPK DSIEKSKVFE ADMLFATLDT TTRAINLLDN
     RLITLTDTVG FVRKLPHELV EAFKSTLEEV IYSEILIHVV DSSAEYVDEQ IEAVEDVLSE
     LGVEDKSMIL ALNKIDNISK EGLEELINRY KEKYQIVSIS AKENINLELL LETIANKLPN
     KLKEVEYVIP YSEQSAVAYL HRNAKIIEST YEDEGTYIKA QVDDEIYNKC RQFIKGI
//
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