IF2_BRADU
ID IF2_BRADU Reviewed; 902 AA.
AC Q89WA9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=bll0783;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC46048.1; -; Genomic_DNA.
DR RefSeq; NP_767423.1; NC_004463.1.
DR RefSeq; WP_011083605.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89WA9; -.
DR SMR; Q89WA9; -.
DR STRING; 224911.27349032; -.
DR EnsemblBacteria; BAC46048; BAC46048; BAC46048.
DR GeneID; 64020648; -.
DR KEGG; bja:bll0783; -.
DR PATRIC; fig|224911.44.peg.158; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR InParanoid; Q89WA9; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q89WA9; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..902
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137177"
FT DOMAIN 398..567
FT /note="tr-type G"
FT REGION 1..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..414
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 432..436
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 509..512
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 545..547
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 509..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 902 AA; 96917 MW; 81D29040A1B6AC2B CRC64;
MVDTKTPGDK KLSVPSKTLS LKPRVETGTV RQSFSHGRSK QVVVEKRGKR RIGDGPEPHA
PEVTAKPAPA APAPSRPAPP PAPPRNAGSG VVLRTLTEDE RSARASALAD AKLREVEERR
QAEEEAQRRA VREAAERAER EAAEARRKAE DERHRHEDEA KRKAETEAKK RFGEGEQPAS
AARPATAAPA APAPRPGAPA ARPGTTTTRP GTTTARPATT TAQRPGAPAG RGPAVAAEPD
EDEAPRQIRR GPGGAARPAP PPKTTHKPGP QKERGRLTVV TALNADEVRE RSIASFRRRT
QRLKGHASNE PKEKLIREVI IPEAITIQEL ANRMAERAVD VIRMLMKQGA MHKITDVIDA
DTAQLIAEEL GHTVKRVAAS DVEEGLFDQV DDSTDTETRS PVVTVMGHVD HGKTSLLDAL
RHANVVSGEA GGITQHIGAY QVVSPESGKK ITFIDTPGHA AFTAMRARGA KVTDIVVLVV
AADDGVMPQT VEAINHAKAA RVPIIVAINK IDKPDAKPER VRTELLQHEV QVESFGGDVV
DVEVSAKNKT NLDKLLEMIA LQADILDLKT NSERPAEGTV IEAKLDRGRG PVATVLVQRG
TLRVGDIIVA GAEMGRVRAL ISDQGETVQE AGPSVPVEVL GFNGPPEAGD RLAVVENEAR
ARQVTSYRAH QKRENAAASI SGMRGSLEQM MSQLKTAGRK EFPLIIKADV QGSLEAILGS
LEKLGTDEVA ARILHAGVGG ISESDVTLAE GFNAAIIGFS VRANKEAAAA AKRNGIEIRY
YNIIYDLVDD VKKAMSGLLA PTLRETMLGN AAILEIFNIS KVGKVAGCRV TDGTVERGAN
VRLIRDNVVV HEGKLSTLKR FKDEVKEVQS GQECGMAFEN YHDMRAGDVI ECYRVETIQR
SL
