IF2_BURVG
ID IF2_BURVG Reviewed; 974 AA.
AC A4JDX1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Bcep1808_1466;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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; CP000614; ABO54474.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JDX1; -.
DR SMR; A4JDX1; -.
DR STRING; 269482.Bcep1808_1466; -.
DR EnsemblBacteria; ABO54474; ABO54474; Bcep1808_1466.
DR KEGG; bvi:Bcep1808_1466; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002287; 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; Reference proteome.
FT CHAIN 1..974
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008217"
FT DOMAIN 474..643
FT /note="tr-type G"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..490
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 508..512
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 529..532
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 583..586
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 619..621
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 116..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..179
FT /note="Basic and acidic 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 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 529..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 583..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 974 AA; 104459 MW; 859A7E5CF36E5E79 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVAEGAEQGQ AQVAEADDDA
ELKRREEEAR REAELLEQQA QELLERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
AAEAAAAQQA AAQQAAEAKQ EAPGAQSAQE EARAAAERAA QREAAKKAED AAREAADKAR
AEQEEIRKRR EAAEAEARAI REMMNTPRKA VVKAVEPPKP VEAPKPAEAK GTLHKPAKPA
GAGVQARPAV KKPAGATPAT TQAPAAGAGD RNKKPGGGKG GWQDDAAKRR GIKTRGDSSG
GVDRGWRGGP KGRGRHQDSA STFQAPTEPI VREVHVPETI SVADLAHKMS IKASEVIKVM
MKMGQMVTIN QVLDQETAMI VVEELGHRAV AAKLDDPEAL LVEGETSSDA EQLPRPPVVT
VMGHVDHGKT SLLDHIRRAK VAAGEAGGIT QHIGAYHVET PRGVITFLDT PGHEAFTAMR
ARGAKATDIV VLVVAADDGV MPQTKEAIAH AKAGGVPIVV AINKIDKPEA NPDRVKQELV
AEGVVPEEYG GDSPFVPVSA KTGAGIDDLL ENVLLQAEVL ELKAPVEAPA KGIVIEAKLD
KGKGPVATIL VQSGTLNRGD IVLAGSAYGR VRAMLDENGK PTKEAGPSIP VEIQGLSEVP
GAGEEVIVLP DERKAREIAL FRQGKFRDVK LAKQQAAKLE SMLEQMGEGE VQNLPLIIKA
DVQGSQEALV QSLLKLSTDE VRVQIVHSAV GGISENDVNL ATASKAVIIG FNTRADAQAR
KLAEANGIDI RYYNIIYDAV DEVKAAMSGM LAPEKREVIT GMVEVRQVFK VPKIGTVAGC
MVTDGIVKRS SSVRVLRNNV VIFTGELESL KRFKDDVKEV KQGFECGMSV KNFNDIVEGD
QFEVFEVTEV ARTL
