IF2_BURTA
ID IF2_BURTA Reviewed; 976 AA.
AC Q2SVG8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BTH_I2564;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000086; ABC36795.1; -; Genomic_DNA.
DR RefSeq; WP_011402420.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SVG8; -.
DR SMR; Q2SVG8; -.
DR PRIDE; Q2SVG8; -.
DR EnsemblBacteria; ABC36795; ABC36795; BTH_I2564.
DR GeneID; 66546964; -.
DR KEGG; bte:BTH_I2564; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001930; Chromosome I.
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..976
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008216"
FT DOMAIN 476..645
FT /note="tr-type G"
FT REGION 48..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..492
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 510..514
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 531..534
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 585..588
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 621..623
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 117..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 531..535
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 585..588
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 976 AA; 104994 MW; 727835628D0C9E48 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
KRKITLTRRH TSEIKQADAT GKARTIQVEV RKKRTFVKRD DVSETGADQA QAQTDEQAEA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRE
AAAAQAEAAQ QAAAAREEAQ RAQSEQSEQS AQDEARAAAE RAAQREAAKK AEDAAREAAD
KARAEQEEIR KRREAAEAEA RAIREMMNTP RRAQVKAVEP PKPAEQPAAK AAEAKGTLHK
PAKPAGEAAA ARPAAKKPAS GAPAPAAAPA GDRNKKPGTG KSGWQDDAAK RRGIKTRGDS
SGGVDRGWRG GPKGRGKHQD SASSFQAPTE PIVREVHVPE TISVADLAHK MAIKASEVIK
VMMKMGQMVT INQVLDQETA MIVVEELGHR ALAAKLDDPE ALLVEGEIGS DAEQLPRPPV
VTVMGHVDHG KTSLLDYIRR AKVAAGEAGG ITQHIGAYHV ETPRGVVTFL DTPGHEAFTA
MRARGAKATD IVILVVAADD GVMPQTKEAI SHAKAGGVPI VVAINKIDKP EANPDRVKQE
LVAEGVVPEE YGGDSPFVPV SAKTGVGIDD LLENVLLQAE VLELKAPVES PAKGIVIEAK
LDKGKGPVAT VLVQSGTLNR GDVVLAGTAY GRVRAMLDEN GKPTKEAGPS IPVEIQGLSE
VPGAGEEVIV LPDERKAREI ALFRQGKFRD VKLAKQQAAK LESMLEQMGE GEVQNLPLII
KADVQGSQEA LVQSLLKLST NEVRVQIVHS AVGGISESDV NLATASKAVI IGFNTRADAQ
ARKLAEANGI DIRYYNIIYD AVDEVKAAMS GMLAPEKREV VTGMVEVRQV FKVPKVGAVA
GCMVTDGVVK RSSSVRVLRN NVVIFTGELD SLKRFKDDVK EVKQGFECGM SIKNFNDIVE
GDQFEVFEVT EVARTL
