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Database: UniProt
Entry: A0A1H4EIN2_9FIRM
LinkDB: A0A1H4EIN2_9FIRM
Original site: A0A1H4EIN2_9FIRM 
ID   A0A1H4EIN2_9FIRM        Unreviewed;       426 AA.
AC   A0A1H4EIN2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=SAMN05216349_13619 {ECO:0000313|EMBL:SEA84737.1};
OS   Oribacterium sp. KHPX15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=1855342 {ECO:0000313|EMBL:SEA84737.1, ECO:0000313|Proteomes:UP000199483};
RN   [1] {ECO:0000313|EMBL:SEA84737.1, ECO:0000313|Proteomes:UP000199483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHPX15 {ECO:0000313|EMBL:SEA84737.1,
RC   ECO:0000313|Proteomes:UP000199483};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006809-2};
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; FNRG01000036; SEA84737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4EIN2; -.
DR   Proteomes; UP000199483; 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   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; GTP-BINDING PROTEIN HFLX; 1.
DR   PANTHER; PTHR10229:SF4; GTPASE HFLX; 1.
DR   Pfam; PF16360; GTP-bdg_M; 1.
DR   Pfam; PF13167; GTP-bdg_N; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006809; GTP-binding_hflX_prd; 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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR006809-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006809-2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000199483}.
FT   DOMAIN          203..373
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   COILED          169..196
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         209..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         241..245
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         263..266
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         329..332
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ   SEQUENCE   426 AA;  48684 MW;  2188D1CFF0783462 CRC64;
     MIDNKELDKK RAILVGACIG NDPDFDTSMR ELEGLAEAEN LEVIADITQN LDSQDSAYYI
     GSGKVQELKA LVWEMEADLV IVNNQLSPSQ LANLAHDLEV EVIDRTNLIL NIFADRARTR
     EAKMQVDYAK LQYMLSRLVG LRQNLSRQGG TGGSMSNKGS GETQIELDRR HIEKQMSELR
     KQLKEISQNR DTQRRKRMTS GIPQVALVGY TNAGKSTLLN KMIKTYCPDE EKEVMVKDML
     FATLDTTVRK ITPPDHRDFL LSDTVGFIND LPHDLVNAFR STLEEAVNAD LILEVIDYSD
     RNYQMHMDVT AKTLKELEAG HIPVLYVMNK SDRKYPEYQL PIDRGDKIYI SAEKGLGLEL
     LLQKIDEKLF SDYLTMELII PYTKGNVEHD LQERARVISV KYEDDGIHMT ADLNQEMIKR
     YKEFIQ
//
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