IF2_SALTO
ID IF2_SALTO Reviewed; 999 AA.
AC A4X4N7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Strop_1370;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP53837.1; -; Genomic_DNA.
DR RefSeq; WP_011905269.1; NC_009380.1.
DR AlphaFoldDB; A4X4N7; -.
DR SMR; A4X4N7; -.
DR STRING; 369723.Strop_1370; -.
DR EnsemblBacteria; ABP53837; ABP53837; Strop_1370.
DR KEGG; stp:Strop_1370; -.
DR PATRIC; fig|369723.5.peg.1396; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000000235; 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; 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..999
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335511"
FT DOMAIN 490..662
FT /note="tr-type G"
FT REGION 50..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..506
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 524..528
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 549..552
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 603..606
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 639..641
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 499..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 549..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 603..606
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 999 AA; 102374 MW; 67D658785B5DDC0F CRC64;
MAGKARVHEL AKELGVESKT VLAKLKEMGE FVKSASSTVE APVARRLRNA FVNNTGSPAP
AAPPAATPPT PTPTPTPPRT PTPAPPPGGP RVTAKPMPPR RPGAPTPGPK PKGPVPGPPQ
SATPAAKPAS AHDIEVAAAE ARAAALKAEQ EAAVKAAQAA RQQQRDNVRR EPPTEGGPRP
GPRPGPGAMP PRPGSPAAGR SGGPTPGPGP RSGGRPPARG AGNNPFGIQG GQQRPPAAGA
GGPRPSPASM PPRPSPASMP PRPSPASMPS QRPGRPGGPG SGRPGAGAGR PGGGGGGGGG
YRGGGGGGGG GYRGGPGGGG GGGGGGGYRG GPGGGGGGFR GGPGGGRPGG GGRGRGGGAA
GAFGRPGGRP TRGRKSKKQR RQEFDNLSAP TMSSGAPRGQ GQTVRLSRGA SLSDFADKIN
ANPGSLVQEM FNLGEMVTAT QSCSDDTLLL LGEHLGFVVQ IVSPEDEDRE LLAQFNIDLD
AEVAEDRLVS RPPVVTVMGH VDHGKTKLLD AIRKANVVAG EAGGITQHIG AYQVHVPHDD
QDRAITFIDT PGHEAFTAMR ARGAQVTDIV ILVVAADDGV MPQTIEALNH AKAADVPIVV
AVNKIDKPDA NPDKVRQQLT EYGLVAEEYG GDTMFVNVAA KPGTGIDSLL EAVLLTADAS
LELTAPTDGP AQGVAIEAHL DKGRGAVATV LVQKGTLRAG DSIVAGGAHG RVRAMLDENG
NQVAEAGPSR PVLVLGLTAV PGAGDTFLAA EDDRTVRQIA EQRQARRRAA AFANSRGRAT
LETLMEQLKA GEKTSLNLVL KGDVSGSVEA LEDALFNLDI PEEVQLRIIH RGVGSITESD
VMLASASSEA VTIIGFNVRA ANKVREMADR EGVEIRYYTV IYQAIEEIEA ALKGLLKPEY
EEVELGTAEV REVFRSSKVG NISGCIVRSG LLRRNAKARL LRDGAVVADN LTIGSLKRFK
DDATEVREGF ECGLTLAGYN NVQVGDVIET FEMREKARV
