ID A0A4S4BWX7_9BACL Unreviewed; 426 AA.
AC A0A4S4BWX7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
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:THF77602.1};
GN ORFNames=E6C55_16335 {ECO:0000313|EMBL:THF77602.1};
OS Cohnella fermenti.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Cohnella.
OX NCBI_TaxID=2565925 {ECO:0000313|EMBL:THF77602.1, ECO:0000313|Proteomes:UP000310636};
RN [1] {ECO:0000313|EMBL:THF77602.1, ECO:0000313|Proteomes:UP000310636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-MHH1044 {ECO:0000313|EMBL:THF77602.1,
RC ECO:0000313|Proteomes:UP000310636};
RA Lin S.-Y., Hung M.-H., Young C.-C.;
RT "Cohnella sp. nov. isolated from preserved vegetables.";
RL Submitted (APR-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THF77602.1}.
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DR EMBL; SSOB01000019; THF77602.1; -; Genomic_DNA.
DR RefSeq; WP_136370902.1; NZ_SSOB01000019.1.
DR AlphaFoldDB; A0A4S4BWX7; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000310636; 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 FunFam; 3.40.50.300:FF:001198; 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; 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 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|ARBA:ARBA00022490, 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:UP000310636}.
FT DOMAIN 198..366
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 157..191
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 204..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 258..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 324..327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 344..346
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 426 AA; 47767 MW; C9C6D7CA6ACC7FFD CRC64;
MEQPNNRAVI VGVNLNDRPD FAYSMEELGN LAEACNIEVV GQLTQNATKI NSSHYLGTGK
IDELSTLALG SDASTVIFND ELSPSQIRNL ESALQKRVID RTILILDIFA ERARTREAQL
QVEVAKLQYM LPRLVGLRES LGRQGGGSGL KNRGAGETKL ELDRRRIEDR IAALQHELEK
LVAQRQVQRK QRRKTGVPVV CLVGYTNAGK SSVMNAVLHR FMQGSGKQVL AQDMLFATLE
TSVRAIELQD NKSFLLTDTV GFVSQLPHYL VKAFRSTLEE VAEADLLIQV VDVSNPEWER
HIEVTNSTLE ELGADGIPMI CACNKSDLTE RAYPRVEEDK VYLSAKQGAG LEELIALVSE
RIFRDYMKCE VVIPFSEGRL VSYFNDNAHV QSIEYEESGT RLTMECKRAD YEKYKEWLVL
PTAAKE
//
