IF2_BURL3
ID IF2_BURL3 Reviewed; 972 AA.
AC Q39H30;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Bcep18194_A4641;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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; CP000151; ABB08236.1; -; Genomic_DNA.
DR RefSeq; WP_011351798.1; NZ_CABVQB010000021.1.
DR AlphaFoldDB; Q39H30; -.
DR SMR; Q39H30; -.
DR EnsemblBacteria; ABB08236; ABB08236; Bcep18194_A4641.
DR GeneID; 45094536; -.
DR KEGG; bur:Bcep18194_A4641; -.
DR PATRIC; fig|482957.22.peg.1551; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002705; 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_0000228180"
FT DOMAIN 472..641
FT /note="tr-type G"
FT REGION 48..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..385
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 48..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 188..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
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; 104295 MW; 7B0DE9139F72105C CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVSEGAEQGQ AQVAEADDDA
ELKRREEEAR READLLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRV
AAEAAAAQQQ AAAQQAAAAE QQEAASTQSA QDEARAAAER AAQREAAKKA EDAAREAADK
ARAEQEEISK RRAAAEAEAR AIREMMNTPR KAVVKAVEPP KPVEPPKPAE AKGTLHKPAK
PEGAQARPAV KKPAGAAAPA TTAPAGAGDR NKKPGAGKGG WQDDASKRRG IKTRGDSSGG
VDRGWRGGPK GRGRHQDSST FQAPTEPIVR EVHVPETVSV ADLAHKMSVK ASEVIKVMMK
MGQMVTINQV LDQETAMIIV EELGHRAVAA KLDDPEALLV EGETGTDAEQ LPRPPVVTVM
GHVDHGKTSL LDHIRRAKVA AGEAGGITQH IGAYHVDTPR GVITFLDTPG HEAFTAMRAR
GAKATDIVVL VVAADDGVMP QTKEAIAHAK AGGVPIVVAI NKIDKPDANL DRVKQELVAE
GVVPEEYGGD SPFVPVSAKT GAGIDDLLEN VLLQAEVLEL KAPVEAPAKG IVIEAKLDKG
KGPVATILVQ AGTLNRGDIV LAGTAYGRVR AMLDENGKPT KEAGPSIPVE IQGLSEVPGA
GEEVIVLPDE RKAREIALFR QGKFRDVKLA KQQAAKLESM LEQMGEGEVQ NLPLIIKADV
QGSQEALVQS LLKLSTDEVR VQIVHSAVGG ISENDVNLAT ASKAVIIGFN TRADAQARKL
AESNGIDIRY YNIIYDAVDE VKAAMSGMLA PEKREVITGM VEVRQVFKVP KIGAVAGCMV
TDGIVKRSSS VRVLRNNVVI FTGELESLKR FKDDVKEVKQ GFECGMSVKN FNDIVEGDQF
EVFEVTEVAR TL
