ID A0A161SMD2_9MICO Unreviewed; 509 AA.
AC A0A161SMD2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KZE92645.1};
GN ORFNames=AVP42_02330 {ECO:0000313|EMBL:KZE92645.1};
OS Agromyces sp. NDB4Y10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE92645.1, ECO:0000313|Proteomes:UP000185889};
RN [1] {ECO:0000313|EMBL:KZE92645.1, ECO:0000313|Proteomes:UP000185889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE92645.1,
RC ECO:0000313|Proteomes:UP000185889};
RA Adelskov J., Patel B.K.;
RT "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT drilled coal seam bore well.";
RL Submitted (JAN-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:KZE92645.1}.
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DR EMBL; LQGY01000050; KZE92645.1; -; Genomic_DNA.
DR RefSeq; WP_067949235.1; NZ_LQGY01000050.1.
DR AlphaFoldDB; A0A161SMD2; -.
DR STRING; 1775951.AVP42_02330; -.
DR PATRIC; fig|1775951.3.peg.2407; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000185889; 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; IPR045498; HflX_C.
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; PF19275; HflX_C; 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:UP000185889}.
FT DOMAIN 287..452
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 54887 MW; B4E5B3025BE4C891 CRC64;
MNDAAHETSD DAVERVLRSA ETRAGIARFG GGDATAIQRD GLDRPGDGDG YDGEQYDREE
RAALRRVGGL STELEDVTEV EYRQLRLENV VLIGVYAQGS LEDAENSLRE LSALAETAGA
RVLDGVLQRR PHPDPSTYLG RGKTEELRHI VAALGADTVV ADTELAPSQR RALEDAVKVK
VIDRTAVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG QVGGAGAGMG
SRGPGETKIE LDRRRIHSRM ARLRKQIAGM KPARDAKRAN RKRNAVPSVA IAGYTNAGKS
SLLNRITGAG VLVENALFAT LDATVRRNTT ADGRVYTIAD TVGFVRNLPH QLVEAFRSTL
EEVADADLVV HVVDAAHPDP ASQIATVRDV IGEVGARDIP ELVVFNKADL ITPEDRLVLQ
GLEPNAVFAS ARTGEGVAEV LEAISRMLPD PAVEVDLLVP YDRGDIVSTL HETGRVLSTE
YVEDGTRIRA LASPEQAAQL AEFRMGALA
//
