HFLX_ALKPO
ID HFLX_ALKPO Reviewed; 423 AA.
AC D3FTV4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900};
DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900};
GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=BpOF4_19480;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}.
CC Note=May associate with membranes. {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP-Rule:MF_00900}.
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DR EMBL; CP001878; ADC51935.1; -; Genomic_DNA.
DR RefSeq; WP_012959297.1; NC_013791.2.
DR AlphaFoldDB; D3FTV4; -.
DR SMR; D3FTV4; -.
DR STRING; 398511.BpOF4_19480; -.
DR PRIDE; D3FTV4; -.
DR EnsemblBacteria; ADC51935; ADC51935; BpOF4_19480.
DR KEGG; bpf:BpOF4_19480; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_2_2_9; -.
DR OMA; AEMKTGR; -.
DR OrthoDB; 1592033at2; -.
DR Proteomes; UP000001544; 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; 3.40.50.11060; -; 1.
DR Gene3D; 3.40.50.300; -; 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 InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR10229; PTHR10229; 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; SSF52540; 1.
DR TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..423
FT /note="GTPase HflX"
FT /id="PRO_0000412654"
FT DOMAIN 201..363
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 207..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 232..236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 254..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 320..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 341..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ SEQUENCE 423 AA; 47943 MW; FD2BDDCE48FDD701 CRC64;
MQDIKQRDIE HVILVGCQVN REDEEFEQSI AELESLAKTA KGKVVGTITQ KREKVESSTY
VGKGKVQELV HLIEETEADL VIFNDELQAS QMRNLHAECG IAVIDRTQLI LDIFASRAKS
REGKLQVELA QLKYLLPRLS GQGLALSRQG GGIGTRGPGE TQLETDRRHI RRRMNEIERQ
LEAVVNHRVR YREKRKKNAA IQLALVGYTN AGKSTLLNRL TKADTLEEDQ LFATLDPTTR
QLHLPSGFSV LMSDTVGFIQ DLPTTLVASF RSTLEELKEA DLLLHVVDCS HPDYEQHERT
VIKLIEELEA HSIPQLLIYN KADQKTDVFI PTHTKDSIIM SAYNEEDLLA LKVKIEQALK
GMMMPYRSII KADEGHILAA ARQETMIHTQ QFDESREAYV IEGHALENTS IYSQLKERLL
KES
