IF2_BURCH
ID IF2_BURCH Reviewed; 971 AA.
AC A0K6X5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Bcen2424_1500;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) 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; CP000458; ABK08252.1; -; Genomic_DNA.
DR RefSeq; WP_011545261.1; NC_008542.1.
DR AlphaFoldDB; A0K6X5; -.
DR SMR; A0K6X5; -.
DR KEGG; bch:Bcen2424_1500; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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..971
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008209"
FT DOMAIN 471..640
FT /note="tr-type G"
FT REGION 48..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..487
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 505..509
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 526..529
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 580..583
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 616..618
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..210
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 480..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 526..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 104278 MW; 90A5E7DB5D59FA23 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVAEGADQGQ AQVAEADDDA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAATKRA
AAEVAAAQQQ AAAQQAAAEQ EATPTQSAQD EARAAAERAA QREAAKKAED AAREAADKAR
AEQEEISKRR AAAEAEARAI REMMNTPRKA VVKAVEPPKP VEPPKPAEAK GTLHKPAKPE
GAQARPAVKK PAGAAAPATT QAPAGAGDRN KKPGAGKGGW QDDAAKRRGI KTRGDSSGGV
DRGWRGGPKG RGRHQDSSTF QAPTEPIVRE VHVPETVSVA DLAHKMSIKA SEVIKVMMKM
GQMVTINQVL DQETAMIIVE ELGHRAVAAK LDDPEALLVE GESGTDAEQL PRPPVVTVMG
HVDHGKTSLL DHIRRAKVAA GEAGGITQHI GAYHVDTPRG VITFLDTPGH EAFTAMRARG
AKATDIVVLV VAADDGVMPQ TKEAIAHAKA GGVPIVVAIN KIDKPEANPD RVKQELVAEG
VVPEEYGGDS PFVPVSAKTG AGIDDLLENV LLQAEVLELK APVEAPAKGI VIEAKLDKGK
GPVATILVQS GTLNRGDIVL AGTAYGRVRA MLDENGKPTK EAGPSIPVEI QGLSEVPGAG
EEVIVLPDER KAREIALFRQ GKFRDVKLAK QQAAKLESML EQMGEGEVQN LPLIIKADVQ
GSQEALVQSL LKLSTDEVRV QIVHSAVGGI SENDVNLATA SKAVIIGFNT RADAQARKLA
EANGIDIRYY NIIYDAVDEV KAAMSGMLAP EKREVITGMV EVRQVFKVPK IGTVAGCMVT
DGIVKRSSSV RVLRNNVVIF TGELESLKRF KDDVKEVKQG FECGMSVKNF NDVTEGDQFE
VFEVTEVART L
