ID F4EVP2_SELS3 Unreviewed; 647 AA.
AC F4EVP2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Selsp_2153 {ECO:0000313|EMBL:AEC01100.1};
OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=546271 {ECO:0000313|EMBL:AEC01100.1, ECO:0000313|Proteomes:UP000011124};
RN [1] {ECO:0000313|EMBL:AEC01100.1, ECO:0000313|Proteomes:UP000011124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28
RC {ECO:0000313|Proteomes:UP000011124};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Selenomonas sputigena DSM 20758.";
RL Submitted (APR-2011) 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; CP002637; AEC01100.1; -; Genomic_DNA.
DR RefSeq; WP_013741050.1; NZ_GG698597.1.
DR AlphaFoldDB; F4EVP2; -.
DR KEGG; ssg:Selsp_2153; -.
DR HOGENOM; CLU_019597_7_1_9; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000011124; Chromosome.
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 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}; 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:UP000011124}.
FT DOMAIN 382..593
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 348..375
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 647 AA; 71287 MW; E4CC1161169A9D06 CRC64;
MKDKRIQGEI QNLKPHIMRE LQSLYDLSVP VGQLSTKELN ERLIAVTEEI GREVAVYVDR
KGRIIEISVG NTWTVDLPAV DARSEVRLSG VRCIHTHPSG DTELSDPDIS SLRRLRFDAM
AAIGRLSGES VGCLGFFTGE KEEDGTLEVQ LFGPVRADHL NRIRLTPLIQ SINKRLSRER
TQATDDEEER AVLAGIDAPM ACALWMTEDS LAELAELART AGATVVGTFI QKKAKPDTAL
FLGRGKVEEM AMFIQNERAT LVIFDDELTP SQQRNLEMAL GVKILDRTAL ILDIFAQRAR
TAAGKLQVEL AQMKYSLPRI LGQGLVLSRL GGGIGTRGPG ETKLEVDRRR IRRRIHDIEG
EIERLKKERL LHRERRRAAR IPVAALVGYT NAGKSTLLNA LTGADVFAED KLFATLDPTT
RSLRLADGRE ILVTDTVGFI QKLPHTLVQA FHATLEEVVE ADILLHVVDV SNEAAEFQIE
AVTEVLKELG AAEKPMLYVL NKLDRLTNGA GGTGGGEAAA HVDTMGDARY EAAGSDAAGG
FSEGEIPSLE EVHLPPAVLR LLRGREGCAI SARTGAGLVE LQERIASFFR TGEVELTLHI
PFTENAAVTR LHEAGRVLQT DYDERGTRVR VRLSEEEAAR FRRYEIS
//
