IF2_MYCTO
ID IF2_MYCTO Reviewed; 900 AA.
AC P9WKK0; L0TAT1; P65131; P71613;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=MT2905;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK47231.1; -; Genomic_DNA.
DR PIR; B70694; B70694.
DR RefSeq; WP_003899505.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WKK0; -.
DR SMR; P9WKK0; -.
DR EnsemblBacteria; AAK47231; AAK47231; MT2905.
DR GeneID; 45426826; -.
DR KEGG; mtc:MT2905; -.
DR PATRIC; fig|83331.31.peg.3138; -.
DR HOGENOM; CLU_006301_9_2_11; -.
DR Proteomes; UP000001020; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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..900
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000427640"
FT DOMAIN 396..567
FT /note="tr-type G"
FT REGION 30..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..412
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 430..434
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 509..512
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 545..547
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 112..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 455..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 509..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 900 AA; 94041 MW; F1B2F3C8A86952C2 CRC64;
MAAGKARVHE LAKELGVTSK EVLARLSEQG EFVKSASSTV EAPVARRLRE SFGGSKPAPA
KGTAKSPGKG PDKSLDKALD AAIDMAAGNG KATAAPAKAA DSGGAAIVSP TTPAAPEPPT
AVPPSPQAPH PGMAPGARPG PVPKPGIRTP RVGNNPFSSA QPADRPIPRP PAPRPGTARP
GVPRPGASPG SMPPRPGGAV GGARPPRPGA PRPGGRPGAP GAGRSDAGGG NYRGGGVGAA
PGTGFRGRPG GGGGGRPGQR GGAAGAFGRP GGAPRRGRKS KRQKRQEYDS MQAPVVGGVR
LPHGNGETIR LARGASLSDF ADKIDANPAA LVQALFNLGE MVTATQSVGD ETLELLGSEM
NYNVQVVSPE DEDRELLESF DLSYGEDEGG EEDLQVRPPV VTVMGHVDHG KTRLLDTIRK
ANVREAEAGG ITQHIGAYQV AVDLDGSQRL ITFIDTPGHE AFTAMRARGA KATDIAILVV
AADDGVMPQT VEAINHAQAA DVPIVVAVNK IDKEGADPAK IRGQLTEYGL VPEEFGGDTM
FVDISAKQGT NIEALEEAVL LTADAALDLR ANPDMEAQGV AIEAHLDRGR GPVATVLVQR
GTLRVGDSVV AGDAYGRVRR MVDEHGEDVE VALPSRPVQV IGFTSVPGAG DNFLVVDEDR
IARQIADRRS ARKRNALAAR SRKRISLEDL DSALKETSQL NLILKGDNAG TVEALEEALM
GIQVDDEVVL RVIDRGVGGI TETNVNLASA SDAVIIGFNV RAEGKATELA SREGVEIRYY
SVIYQAIDEI EQALRGLLKP IYEENQLGRA EIRALFRSSK VGLIAGCLVT SGVMRRNAKA
RLLRDNIVVA ENLSIASLRR EKDDVTEVRD GFECGLTLGY ADIKEGDVIE SYELVQKERA
