IF2_LIMF3
ID IF2_LIMF3 Reviewed; 775 AA.
AC B2GBN7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LAF_0733;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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; AP008937; BAG27069.1; -; Genomic_DNA.
DR RefSeq; WP_012391101.1; NC_010610.1.
DR AlphaFoldDB; B2GBN7; -.
DR SMR; B2GBN7; -.
DR EnsemblBacteria; BAG27069; BAG27069; LAF_0733.
DR GeneID; 61201018; -.
DR KEGG; lfe:LAF_0733; -.
DR PATRIC; fig|334390.5.peg.795; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001697; 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 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..775
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093797"
FT DOMAIN 276..445
FT /note="tr-type G"
FT REGION 29..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..292
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 310..314
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 331..334
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 385..388
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 421..423
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 331..335
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 385..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 775 AA; 84641 MW; A5BAE5E965F5169E CRC64;
MAKERIYELA KELKMPSKDL VNLAKKEGMD VKTHMSSVTS DEANKLRSMA KGAGKPAAVK
PAPKVQEHQS APAKKEASRP ANQGSQNNQN RNNRGNRNNN GNNNRHNSNN GSANANGNGG
NQKRNQKRNQ NNNNQGGQAA NRNNNNGQGQ GAHWFKKGKK NNKKKNRNKG NQRLRDTAPK
APTQRKDRPL PDVLEYTNGM NAQDLGKILH RSPAEIIKKL FMLGVMVNQN QSLDADTIEI
LAADYGIGAK EKVQVDVADL DHFFDERINN DANLADRPPV VTVMGHVDHG KTTLLDKIRH
SHVTEGEAGG ITQAIGAYQV KYNDKLITFL DTPGHAAFTE MRARGANITD ITVLVVAADD
GVMPQTIEAI NHAKAAGTPI IVVVNKIDKP GANPDHVTEQ LTEYGLIPED WGGDTIYVKV
SAKFGKNIDE LLDMILLQAE VMELKANPGQ NAAGAVVEAR LDQGKGSVAT LLVQQGTLHV
GDPIVVGDTF GRVRTMTNEN GRRIKDATPS TPVEITGLNG VPEAGDHFVV FDDEKTARAA
GEERAKRAED EKRRRTSHVT LDNLFDTMKK GEMKSLPIII KADVQGSVEA LAQSLQKIQV
DGVRVDIIHK AVGAISESDV TLAEASNAII IGFNVRPTPL AKSEAETNNI DIRLHRVIYN
AIEEVEDAMK GMLEPVYEEE VLGQVEVRQL YKASKIGTIA GGMVVSGKIT RDAKVRLIRD
GVVIYEGELG SLKRFKDDAK EVKMGFECGL TIKNFNDVKE NDVIEAYHMK EVPVK
