IF2_BURA4
ID IF2_BURA4 Reviewed; 972 AA.
AC B1YP36;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=BamMC406_1422;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001025; ACB63910.1; -; Genomic_DNA.
DR RefSeq; WP_012363741.1; NC_010551.1.
DR AlphaFoldDB; B1YP36; -.
DR SMR; B1YP36; -.
DR EnsemblBacteria; ACB63910; ACB63910; BamMC406_1422.
DR KEGG; bac:BamMC406_1422; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001680; Chromosome 1.
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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR SUPFAM; SSF46955; SSF46955; 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..972
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093761"
FT DOMAIN 472..641
FT /note="tr-type G"
FT REGION 49..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..488
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 506..510
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 581..584
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 617..619
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 581..584
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 972 AA; 104345 MW; B0C5C3F44E124155 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE ADKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVAEGAEQGQ AQVAEADDDA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
AAAAVEAQQA AAQQAAEAQQ ETAGAQSAQD EARAAAERAA QREAAKKAED AAREAADKTR
AEQEEIRKRR EAAEAEARAI REMMNTPRKA VVKAVEPPKP VEPPKPVEAK GTLHKPAKPA
GAGAARPAVK KPAGAAPATT QAPAGAGDRN KKPGGGKGGW QDDAAKRRGI KTRGDSSGGV
DRGWRGGPKG RGRHQDSAST FQAPTEPIVR EVHVPETVSV ADLAHKMSIK ASEVIKVMMK
MGQMVTINQV LDQETAMIVV EELGHRAVAA KLDDPEALLV EGEATTDAEQ LPRPPVVTVM
GHVDHGKTSL LDHIRRAKVA AGEAGGITQH IGAYHVETPR GVITFLDTPG HEAFTAMRAR
GAKATDIVVL VVAADDGVMP QTKEAIAHAK AGGVPIVVAI NKIDKPEANP DRVKQELVAE
GVVPEEYGGD SPFVPVSAKT GVGIDDLLEN VLLQAEVLEL KAPIEAPAKG IVIEAKLDKG
KGPVATILVQ SGTLNRGDVV LAGSAYGRVR AMLDENGKPT KEAGPSIPVE IQGLSEVPGA
GEEVIVLPDE RKAREIALFR QGKFRDVKLA KQQAAKLESM LEQMGEGEVQ NLPLIIKADV
QGSQEALVQS LLKLSTDEVR VQIVHSAVGG ISENDVNLAT ASKAVIIGFN TRADAQARKL
AESNGIDIRY YNIIYDAVDE VKAAMSGMLA PEKREVITGM VEVRQVFKVP KIGTVAGCMV
TDGIVKRSSS VRVLRNNVVI FTGELESLKR FKDDVKEVKQ GFECGMSVKN FNDVIEGDQF
EVFEVTEVAR TL
