ID A0A1G9MLX4_9CLOT Unreviewed; 599 AA.
AC A0A1G9MLX4;
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=SAMN04487833_13017 {ECO:0000313|EMBL:SDL75134.1};
OS Sarcina sp. DSM 11001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Sarcina.
OX NCBI_TaxID=1798184 {ECO:0000313|EMBL:SDL75134.1, ECO:0000313|Proteomes:UP000199127};
RN [1] {ECO:0000313|EMBL:SDL75134.1, ECO:0000313|Proteomes:UP000199127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11001 {ECO:0000313|EMBL:SDL75134.1,
RC ECO:0000313|Proteomes:UP000199127};
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 -!- 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; FNFZ01000030; SDL75134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9MLX4; -.
DR STRING; 1798184.SAMN04487833_13017; -.
DR Proteomes; UP000199127; 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; 2.
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:UP000199127}.
FT DOMAIN 302..545
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..295
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65723 MW; F54DFC6F17B5932E CRC64;
MKHNDGSDHS RADTDLIISW GKNKYVRAGS APETKEVPEK PKVPYRLEMP EVPHGSERPE
VPHGSERPEV PHGSERPEVP RRAAGSSEPE IPRRTSRSSG PEPAEKGSRA ILAGCNTGTD
AGKYARAMAE LRGLAEACGL KAVSVLVQNA PAVTHATYIG SGKVLELKKE VEEFDADIVL
FNEALTPMQT RNLEKVLDTE VLDRTGLILQ IFALRARTRE AKLQVESAQL QYMLPRLAGM
RTNLSRQGGG SGRLSNKGAG EQKLELDRRR IEHRIAELRR ELDVVSRERA TQRNRRMRTG
MTRVALVGYT NAGKSTVMNA LLKYCAGTSG SGTGSFSPAD RSPLSGSLKN TDPAGESFCD
SAAKGSFKDP SNISAPISQD RMSSPDTAEQ AGGKTVFEAD MLFATLDTSV RRIDAPGHIP
FLLSDTVGFV SDLPHALVKA FRSTLDEVCC ADLLLEVVDF SDPDYRRQIE VTARTLEEIG
AGHIPVVYLY NKVDLALREE ASEKDRPVPL RIPYRRGEIL YLAAGKKIGI PDILTLIDDA
LEESRTETGF LIPYKKGALL QEIRSCGVLL SEEYLPEGIR VRARCRREDA LRISRLCGE
//
