IF2_BEII9
ID IF2_BEII9 Reviewed; 1053 AA.
AC B2IIJ7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bind_1047;
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) 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; CP001016; ACB94690.1; -; Genomic_DNA.
DR RefSeq; WP_012384047.1; NC_010581.1.
DR AlphaFoldDB; B2IIJ7; -.
DR SMR; B2IIJ7; -.
DR STRING; 395963.Bind_1047; -.
DR EnsemblBacteria; ACB94690; ACB94690; Bind_1047.
DR KEGG; bid:Bind_1047; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 129583at2; -.
DR Proteomes; UP000001695; Chromosome.
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; 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; 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..1053
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117324"
FT DOMAIN 550..720
FT /note="tr-type G"
FT REGION 1..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..566
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 584..588
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 606..609
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 660..663
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 696..698
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 559..566
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 606..610
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 660..663
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1053 AA; 111003 MW; B891FD9116619B04 CRC64;
MSESKNSGEN TLSVTPTKTL SLKRPVEAGT VRQSFPHGRS KAVVVEKVKR RPIGPGGDGH
PAREAAPTPA PAATVTAPPP AQRPAAPNPT AAPTTPPAAA VPNVPPPAPR AEVAPPSAQP
APAAPTAATP PAQPKAEPVP APIAAQAAPA PVPPVPAPSA PVPSTSAAPA APKPAPAPVS
QAKPIQTAPV QTAPAAQASA SQTTGPRPVA AGPRPATGAA KQATATPQRG AASPAQRPQT
GGGQRSGGQQ RNQSGGRGGP GRGESGSSRT PTGVVLRSLT DEEREARARA LSGARIREEE
DRKRAAAEAK AREEREARER EERAAAEARK AEEDARRLQE QEAKRRSEQE AKRRLSGGEP
APAASPSVAR KPVMTATAAA PAAAAPSGRA AVTDEEETKR VIRRPGMPTK VIVPPRPTKG
AEPKSRGRLT VATATGGEEE ERTRSVAAFR RRQQRLRGHV NEVKEKLSRE VILPETITIQ
ELANRMSERG VDVIKLLMKQ GQMAKITDVI DADTAQLIAE ELGHTVKRVA ESDVEEGLFD
TVDVEEHLVP RPPVVTIMGH VDHGKTSLLD AIRHANVVSG EAGGITQHIG AYQITAPNGS
PITFIDTPGH AAFTAMRARG AKVTDIVVLV VAADDGVMPQ TAEAVAHARA AGVPIIVAIN
KIDKPDAKPE RIRSELLQYE VQVESLGGDT LEVEVSATKK INLDKLLDLI ALQAELLDLK
ANPDRAAEGT VIEASLDKGR GPVATVLVQR GTLRVGDIIV GGTHWGHVRA LIDDKGATRS
EAGPSMPVEV LGFSGSPEAG DRVAVVETEA RAREITEYRE RQRREQAAAR GGQARGSLAD
MMSQLKNAGR KEFPLVIKGD VQGSVEAVVA TLEKLNTDEV AARIIHAGVG GITESDITLA
QAAGAVVLGF NVRALKEARA LAEQQGIEIR YYNIIYNLVD DVKAAMSGLL APTLREEMLG
NAEILEVFNI SKVGKVAGCR VTDGRVERGA HVRLIRDNVV VHEGKLSTLK RFKDEVKEVV
AGQECGMAFE SYQDMRPHDV IECYNVHEIK RSL
