IF2_BRASB
ID IF2_BRASB Reviewed; 921 AA.
AC A5E866;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BBta_0057;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
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; CP000494; ABQ32360.1; -; Genomic_DNA.
DR RefSeq; WP_011942584.1; NC_009485.1.
DR AlphaFoldDB; A5E866; -.
DR SMR; A5E866; -.
DR STRING; 288000.BBta_0057; -.
DR PRIDE; A5E866; -.
DR EnsemblBacteria; ABQ32360; ABQ32360; BBta_0057.
DR KEGG; bbt:BBta_0057; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000246; 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; 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.
FT CHAIN 1..921
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008206"
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 20..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 102..181
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; 98697 MW; 5D6CF382896395CC CRC64;
MADNNTPGDK KLSVPTKTLT LKPRVETGTV RQSFPHGRSK QVVVEKRGTK RRVGDGAPDA
PHAPEPVVAK APPPPPPSNR PSGPRPGSSQ RGGSGVVLRT LTEDERSARA SALADARVRD
MEERRQAEEE ARRRAEREAA ERAEREAAEA RRKAEEERHR QEEEAKRKAE LEAKKRFGEG
EAPRPATAAP QQQPAAVTAP ARPAQAPGRP QGAPGSRPQQ IGTSARPGGA QPAGARPAAA
RPAGAGPLGR APGVAAGPED DEGPRQIRRG PGGAARPAPP PKTTHKPGPQ KQRGRLTVVT
ALTADDVRER SIASFRRRTQ RLKGHAANEQ KEKLVREVTI PEAITIQELA NRMSERAVDV
IRLLMRQGAM HKITDVIDAD TAQLIAEELG HSVKRVAASD VEEGLFDVVD DSTDTEPRSP
VVTVMGHVDH GKTSLLDALR HANVVSGEAG GITQHIGAYQ VTAPDSGKKI TFIDTPGHAA
FTAMRARGAK VTDIVVLVVA ADDGVMPQTI EAINHAKAAK VPMIVAINKI DKPDARPDRV
RTELLQHEVQ VESLGGEVVD VEVSAKNKTN LDRLLEMIAL QADILDLKTN SDRPAEGTVI
EAKLDRGRGP VATVLVQRGT LRVGDIIVAG AEMGRVRALI SDQGETLQEA GPSVPVEVLG
FNGPPEAGDR LAVVENEARA RQVTSYRAHQ KRENAAASIS GMRGSLEQMM SQLKTAGRKE
FPLVIKADVQ GSLEAILGSL EKLGTDEVAA RILHAGVGGI SESDVTLAEG FNAAIIGFSV
RANKEAAALA KRNGIEIRYY NIIYDLVDDV KKAMSGLLAP TLRETMLGNA QILEVFNISK
VGKVAGCRVT DGTVERGANV RLIRDNVVVH EGKLSTLKRF KDEVKEVQAG QECGMAFESY
GDMRVGDVIE CYRVETIQRS L
