IF2_BURM1
ID IF2_BURM1 Reviewed; 969 AA.
AC A9ABD5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Bmul_1755, BMULJ_01485;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-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; CP000868; ABX15443.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG43414.1; -; Genomic_DNA.
DR RefSeq; WP_006402062.1; NC_010804.1.
DR AlphaFoldDB; A9ABD5; -.
DR SMR; A9ABD5; -.
DR STRING; 395019.Bmul_1755; -.
DR EnsemblBacteria; BAG43414; BAG43414; BMULJ_01485.
DR KEGG; bmj:BMULJ_01485; -.
DR KEGG; bmu:Bmul_1755; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000008815; 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..969
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093764"
FT DOMAIN 469..638
FT /note="tr-type G"
FT REGION 49..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..485
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 503..507
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 578..581
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 614..616
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 143..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..528
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 578..581
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 969 AA; 103900 MW; 8B9F7A410DF2CFBF CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE ADKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVSDVAEQGQ AQVAEADDDA
ELKRREEEAR REAALLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
AAEAAAAQQA AQQAAAAQQA AAPADSAQDE ARAAAERAAQ REAAKKAEDA AREAAEKARA
EQEEIRKRRE AAEAEARAIR EMMNTPRKAV VKAVEPPKPA EPAKPAEAKG TLHKPAKPEG
AQARPAAKKP AAAPAATPAP AGAGDRNKKP GGGKGGWQDD AAKRRGIKTR GDSSGGVDRG
WRGGPKGRGR HQDNASSFQA PTEPIVREVH VPETISVADL AHKMAIKASE VIKVMMKMGQ
MVTINQVLDQ ETAMIVVEEL GHRALAAKLD DPEALLVEGE TGSDAEQLPR PPVVTVMGHV
DHGKTSLLDY IRRAKVAAGE AGGITQHIGA YHVETPRGVV TFLDTPGHEA FTAMRARGAK
ATDIVILVVA ADDGVMPQTK EAISHAKAGG VPIVVAINKI DKPEANPDRV KQELVAEGVV
PEEYGGDSPF VPVSAKTGAG IDDLLENVLL QAEVLELKAP VEAPAKGIVI EAKLDKGKGP
VATMLVQSGT LSRGDIVLAG TAYGRVRAML DENGKPTKEA GPSIPVEIQG LSEVPAAGEE
VIVLPDERKA REIALFRQGK FRDVKLAKQQ AAKLESMLEQ MGEGEVQNLP LIIKADVQGS
QEALVQSLLK LSTDEVRVQI VHSAVGGISE SDVNLATASK AVIIGFNTRA DAQARKLAEA
NGIDIRYYNI IYDAVDEVKA AMSGMLAPEK REVVTGMVEV RQVFKVPKVG TVAGCMVTDG
IVKRSSSVRV LRNNVVIFTG ELESLKRFKD DVKEVKQGFE CGMSVKNFND ILEGDQFEVF
EVTEVARTL
