ID B2GKG6_KOCRD Unreviewed; 552 AA.
AC B2GKG6;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
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:BAG29925.1};
GN OrderedLocusNames=KRH_15780 {ECO:0000313|EMBL:BAG29925.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG29925.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG29925.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG29925.1; -; Genomic_DNA.
DR AlphaFoldDB; B2GKG6; -.
DR STRING; 378753.KRH_15780; -.
DR KEGG; krh:KRH_15780; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_7_0_11; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000008838; 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 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:UP000008838}.
FT DOMAIN 317..482
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 60008 MW; 487EA4508FB91719 CRC64;
MTDTSSHRNH ASDEPGRSGD LTGSELEDVV SRVLARARSR TEPVVTADGH VPEDDAAAPR
AGHERLGRAR ELADEDDVHV PSDGDQQDLA ERHALRRVAG LSTELEDVTE VEYRQLRLER
VVLAGLYSSG TLAEAENSLR ELAALAETAG SEVMDGMLQR RVNPDPGTYL GSGKALELKD
VVAATGADTV IVDAELAPSQ RRALEDVVKV KVIDRTGLIL DIFAQHAKSK EGKAQVELAQ
LEYMLPRLRG WGESLSRQAG GRAASGEGIG SRGPGETKIE LDRRRIRQRM AKLRREIAAM
KPARETKRLN RRRNAVPSVA IAGYTNAGKS SLLNRLTDAG VLVENALFAT LDPTVRKAQT
PDGIGYTLAD TVGFVRSLPT QLVEAFRSTL EEVADADVIV HVVDASHPDP EGQLKAVRDV
LTDVGANDIP EIVALNKSDI ADPVVLARLR NHESPSVAVS ARTGEGIEEL RRMISAAIPR
PNHDLDLLVP YVHGEVVSRL HAQDAEILST EHTPDGTRLH VRVREDLVED LQQYRSDRPQ
PHDVGEQDTQ GA
//
