IF2_GLUDA
ID IF2_GLUDA Reviewed; 907 AA.
AC A9HF18; B5ZDK0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=GDI1365, Gdia_2070;
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: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; AM889285; CAP55308.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI51830.1; -; Genomic_DNA.
DR RefSeq; WP_012224611.1; NC_011365.1.
DR AlphaFoldDB; A9HF18; -.
DR SMR; A9HF18; -.
DR STRING; 272568.GDI1365; -.
DR EnsemblBacteria; ACI51830; ACI51830; Gdia_2070.
DR EnsemblBacteria; CAP55308; CAP55308; GDI1365.
DR KEGG; gdi:GDI1365; -.
DR KEGG; gdj:Gdia_2070; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG5373; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..907
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075607"
FT DOMAIN 406..576
FT /note="tr-type G"
FT REGION 1..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..422
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 440..444
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 462..465
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 516..519
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 552..554
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 92..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 462..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 516..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 907 AA; 97865 MW; 1062C2E303830C71 CRC64;
MSEGNDQDQG KGRLSLRPAG RKDVGRTVDA GSVRQSFSHG RSKVVQVEVR KKRGPGPAPA
GSGSGSSGGG RAGGRGGSGG RALTASELAT RQRVLEEQRA EAVRREQERR EQEKIMILSA
AEEARRRDEE ARRAAEDEVR EKEEAAARAR EEEAERRASA QAHGQAGTPS RAEPEPESSG
PVVSAVPIPG AVTLAPPMER LRPLAERAIM PARPVTPSRP ATPAATPQAP GETLRLRTGR
VGEAEDDRRP ARRPGGGIAP GRKPSGASPK KGGDSRRSGR IDVQAAIEGD DDKTRSLASV
RRQRERERRQ AELERLRADQ VRVVRDVILP ETITVQELAN RMAARQGEVI KALMKMGVMA
TVTQSLDADT AELVVQEFGH RVRRVADSDV EIGIEGIEDQ PEDLLPRPPV VTVMGHVDHG
KTSLLDALRT TDVAAAEAGG ITQHIGAYQV TLPSGSKITF IDTPGHEAFT AMRARGASVT
DVVVLVVAAD DGVMPQTIEA IRHAKAANAP IIVAINKCDK PGANPERVRQ ELLSHEIVVE
SMGGDTQDVE VSALKRTGLD KLEEAILLQA EMLDLRANPD RVAEGSVIES RLDRGRGPVA
TVLVQKGTLR RGDIVVAGAE WGRVRAMLDD RGRQIQEAAP AMPVEILGIA GVPGAGEPFV
VVDNENRARE ISEFRQRVIR DRTAAGQTAA RGTLDQMLAR IQAGAQKEVA VLIKADVQGS
AEALQATVLK LEHEEVKVRV LTAGVGQITE SDVQLAKASD AVIIAFNVRA TTQARELAQR
EGVDIRYYSI IYQVADDVEQ LVKGKVAPKH REKFLGYAEI RKVFDITKVG KVAGCYVTEG
VVKRGCGVRL LRDNVVVHEG ELSQLKRFKD DVKEVARGYE CGLSFAGYND LREGDMVECY
EMELVPA
