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HFLX_GLUDA
ID   HFLX_GLUDA              Reviewed;         450 AA.
AC   A9H253; B5ZEJ7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=GDI0162, Gdia_2232;
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA   Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA   Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA   Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA   Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA   Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA   Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=21304715; DOI=10.4056/sigs.972221;
RA   Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT   "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT   diazotrophicus PAl 5, suggest a new standard in genome sequence
RT   submission.";
RL   Stand. Genomic Sci. 2:309-317(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP54105.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AM889285; CAP54105.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001189; ACI51987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9H253; -.
DR   SMR; A9H253; -.
DR   STRING; 272568.GDI0162; -.
DR   EnsemblBacteria; ACI51987; ACI51987; Gdia_2232.
DR   EnsemblBacteria; CAP54105; CAP54105; GDI0162.
DR   KEGG; gdi:GDI0162; -.
DR   KEGG; gdj:Gdia_2232; -.
DR   eggNOG; COG2262; Bacteria.
DR   HOGENOM; CLU_019597_2_1_5; -.
DR   Proteomes; UP000000736; Chromosome.
DR   Proteomes; UP000001176; 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   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   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..450
FT                   /note="GTPase HflX"
FT                   /id="PRO_0000412658"
FT   DOMAIN          230..395
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   REGION          79..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         236..243
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         261..265
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         283..286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         349..352
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         373..375
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   CONFLICT        103..105
FT                   /note="PEP -> AEA (in Ref. 2; ACI51987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="S -> T (in Ref. 2; ACI51987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="A -> T (in Ref. 2; ACI51987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        376..378
FT                   /note="APG -> TPA (in Ref. 2; ACI51987)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  48648 MW;  36A8F244A9E7C74C CRC64;
     METKPPIPLA VLVGIQTPDV DDIAHEASLA ELGRLVKTLG YAVVGTVSQK REGTGAALLL
     GSGKLAELAA LTGGTGVVTS MAPPPKSKAR QRFEGAAEGA APPEPDPDAA RRPEFVIVDH
     ELSPSQIRNL ERATGAQVLD RTGVIVEIFH RHANTREARL QVEMARLKYV APRLRESSGG
     GGRQQGPGAG ESTLALDRRK IRDRLAELKT QLDAVQRDGD QRRSARRDQL RVALVGYTNA
     GKSSLMRALT GSQVLVEDKL FATLDTTVRI LQPETRPRIL VSDTVGFIKQ LPHDLVASFR
     STLAEALEAS LLLFVVDASD PTYESQLEVT RGVLREIGAD AVPSRLVLNK MDRLDPAARA
     ALRDKHPDAI MLSAHAPGDV SALRDTLIAF FEAEMVEDTL VLPYAKQGLI GEIYESARVL
     SEDHDETGRV LKVRALPAAI TRLKRSLAAR
 
 
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