ID A0A1Q8QVU1_9FIRM Unreviewed; 536 AA.
AC A0A1Q8QVU1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=DSOL_2634 {ECO:0000313|EMBL:OLN31461.1};
OS Desulfosporosinus metallidurans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN31461.1, ECO:0000313|Proteomes:UP000186102};
RN [1] {ECO:0000313|EMBL:OLN31461.1, ECO:0000313|Proteomes:UP000186102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL {ECO:0000313|EMBL:OLN31461.1,
RC ECO:0000313|Proteomes:UP000186102};
RA Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT "Complete genome of Desulfosporosinus sp. OL.";
RL Submitted (SEP-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}.
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:OLN31461.1}.
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DR EMBL; MLBF01000018; OLN31461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8QVU1; -.
DR STRING; 1888891.DSOL_2634; -.
DR Proteomes; UP000186102; 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: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 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:UP000186102}.
FT DOMAIN 366..536
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 325..352
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 536 AA; 59946 MW; 9A1FE4272F3F17B6 CRC64;
MDMDISGDLS GIRDSQLQEL KNLSEFKTER SELIQPNILE ELLRLTQLWN REIAIYLSRP
GILLAAAVGR SASVTLPPIK GRSLGKHLRC IHTHPNGDFR LSQLDLSALT SLQLESMSSV
GVRDGKLTGI QIAYSSGEND PFILNINSKN WQSFDYNESL SNVSKGLTKT VTAHSKERAF
LIALEDSDQE INEDLLELRE LARSAGVDVV GQLVQNRRYG QSRSYLGSGK LEELIHHLQE
TEANVVICDD ELSPTQLRTL EMETGVKVLD RTGLILDIFA QRAQSREGKL QVELAQLKHL
LPYLSGQGQA LSRLGAGVGS RGPGETKLEL DRRRMRERIT QLEKELKLVL QHRDVQRRQR
TRSGLPAIAL VGYTNAGKTT FMKIAMEQAG TRSDIPIGEN KLFATLDPIV RRIRVNSTME
ILLSDTVGFI RKLPTQLLRA FLATLEEVQQ ADILLHVLDA SHPQAFQHAE TVQQVLKQLG
CAEKPMMTLL NKADKVLVEE DLKQLAQSLP YPIEMSLIRG DSLKPVWKVC DSLLTY
//
