ID F8ESH4_ZYMMT Unreviewed; 458 AA.
AC F8ESH4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=Zymop_0849 {ECO:0000313|EMBL:AEI37749.1};
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI37749.1, ECO:0000313|Proteomes:UP000000491};
RN [1] {ECO:0000313|EMBL:AEI37749.1, ECO:0000313|Proteomes:UP000000491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC NCIMB 11200 / NRRL B-4491 / Barker I
RC {ECO:0000313|Proteomes:UP000000491};
RX PubMed=21742897; DOI=10.1128/JB.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(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:0000256|HAMAP-Rule:MF_00900}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR006809-2};
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; CP002865; AEI37749.1; -; Genomic_DNA.
DR RefSeq; WP_013934145.1; NC_015709.1.
DR AlphaFoldDB; F8ESH4; -.
DR STRING; 579138.Zymop_0849; -.
DR KEGG; zmp:Zymop_0849; -.
DR PATRIC; fig|579138.3.peg.893; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_1_0_5; -.
DR Proteomes; UP000000491; 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; 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 PIRSF; PIRSF006809; GTP-binding_hflX_prd; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR006809-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006809-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00900}.
FT DOMAIN 209..385
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT BINDING 215..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 240..244
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 262..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 336..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 458 AA; 50773 MW; A4AE9B53D3136078 CRC64;
MSGFVRSDAD GVSQGARILV VLPELEDNNR RSTEARLEEA TGLAHAIGLD VVAKLAFRLR
SPKAATLFGQ GQVDQIVTAA KDEEIDLVVV DGPLTPIQQR NLETALDVKV IDRTGLILEI
FGARAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD
RMAKLRRDLA QVTRTRGLHR ARRKRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAKDLLF
ATLDPTMRQI ELPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTAADL ILHVRDIAQP
DSDSERDDVE RVLAEIGIAP VEEGGEFAIP IIEAWNKSDL LSEEAHESLA AEASRREDVA
LISAWTGEGI ESLRHLISER LSNAHRLRHI DLPSTEGQAM AWLHAHGEVV NQTMNDQAQM
EFDVRMSDEN WGRFIERFGF LYNDETTLKN EKEGLHPL
//
