IF2_BRASO
ID IF2_BRASO Reviewed; 921 AA.
AC A4YJE9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BRADO0053;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL74025.1; -; Genomic_DNA.
DR RefSeq; WP_011923327.1; NC_009445.1.
DR AlphaFoldDB; A4YJE9; -.
DR SMR; A4YJE9; -.
DR STRING; 114615.BRADO0053; -.
DR EnsemblBacteria; CAL74025; CAL74025; BRADO0053.
DR KEGG; bra:BRADO0053; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; BSP114615:BRADO_RS00265-MON; -.
DR Proteomes; UP000001994; 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..921
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008207"
FT DOMAIN 417..586
FT /note="tr-type G"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..433
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 451..455
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 474..477
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 528..531
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 564..566
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 474..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 528..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 921 AA; 98625 MW; F94D6A5835AAC2DA CRC64;
MADQNTPGDK KLGVPSKTLT LKPRVETGTV RQSFPHGRSK QVVVEKRGTK RRVGDGAPDA
PHAPEPTVAK APPPPPPSNR PSGPRPSGGQ QRGGSGVVLR TLTEDERSAR ASALADARVR
DLEERRQAEE EARRRAEREA AERAEREAAE ARRKAEEERH RHEEEAKRKA ELEAKKRFGE
GEAPRPAAAA PQPTVSAPAR PAQAPGRPQG APGSRPQQIG GPSSRPGGSQ PGGARPAGPR
PAGGGPLGRA PAAVAAGPDE DEGPRQIRRG PGGAARPAPP PKTTHKPGPQ KQRGRLTVVT
ALNADDVRER SIASFRRRTQ RLKGHAANEQ KEKLVREVTI PEAITIQELA NRMSERAVDV
IRLLMRQGAM HKITDVIDAD TAQLIAEELG HTVKRVAASD VEEGLFDVVD DSTDTEPRSP
VVTVMGHVDH GKTSLLDALR HANVVSGEAG GITQHIGAYQ VTAPDSGKKI TFIDTPGHAA
FTAMRARGAK VTDIVVLVVA ADDGVMPQTI EAINHAKAAK VPMIVAINKI DKPDARPERV
RTELLQHEVQ VESLGGDVVD VEVSAKNKTN LDRLLEMIAL QADILDLKTN SDRPAEGTVI
EAKLDRGRGP VATVLVQRGT LRVGDIIVAG AEMGRVRALI SDQGETLQEA GPSVPVEVLG
FNGPPEAGDR LAVVENEARA RQVTSYRAHQ KRENAAASIS GMRGSLEQMM SQLKTAGRKE
FPLVIKADVQ GSLEAILGSL EKLGTEEVAA RILHAGVGGI SESDVTLAEG FNAAIIGFSV
RANKEAAALA KRNGIEIRYY NIIYDLVDDV KKAMSGLLAP TLRETMLGNA QILEVFNISK
VGKVAGCRVT DGTVERGANV RLIRDNVVVH EGKLSTLKRF KDEVKDVQAG QECGMAFENY
GDMRVGDVIE CYRVETIQRS L
