IF2_FRATN
ID IF2_FRATN Reviewed; 846 AA.
AC A0Q8F3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-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=FTN_1660;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000439; ABK90518.1; -; Genomic_DNA.
DR RefSeq; WP_003041281.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q8F3; -.
DR SMR; A0Q8F3; -.
DR EnsemblBacteria; ABK90518; ABK90518; FTN_1660.
DR GeneID; 60805977; -.
DR KEGG; ftn:FTN_1660; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; FTUL401614:G1G75-1721-MON; -.
DR Proteomes; UP000000762; 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; IPR009061; DNA-bd_dom_put_sf.
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; 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.
FT CHAIN 1..846
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335470"
FT DOMAIN 345..512
FT /note="tr-type G"
FT REGION 198..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..361
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 379..383
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 400..403
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 490..492
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 354..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 400..404
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 846 AA; 92306 MW; 57149D10D9F22654 CRC64;
MAEITVGQLA QQTNKEVDAL LKQLKSFGIE KSSEKDTLTP AEMKTLLEKI NSAKNTATRK
KVTSVKLDGK HKINVSVKRK RRVAKKVEQQ ESTTLEQPQE LETMVQEVSQ QVDIVKGQDN
IEQIVENKEA VKVQEQRQAE IAKPVIKDSG FKITAMPEIK IEEIVTEDDE GLSASDKQAK
KKAAKKVFSE AVNTNTKYKR EEEEKKSKAK KAGGKGFKKA NPRQLSQLAG DLESFDEFGA
KKGKLKAPKV KKQEFTKPVE NTVRTVEIHE GITVSELAQK MAVKGAEIVK VLFNMGVMAT
INQSLDQDTA ILIVEEMGHK YTLHNENALE EAVTTVDRSS YKKISRAPVV TIMGHVDHGK
TSLLDYIRQT RVVAGEAGGI TQHIGAYSVK TDKGSITFLD TPGHEAFTSM RARGAKSTDI
VILVVAADDG VMPQTEEAIQ HAKAARVPIV VAVNKIDKPE ADPDKVISEL AQRNVIPESW
GGDVMFVNVS AKTGEGVADL LEAVLLQSEV LELEAFAEGL AEGVVIESRL EKGRGPVATV
LVQNGNLKQG DNILCGTEYG RVRAMHNDLG KKIKAAGPAT PVEILGLSGV PAAGDEMVVI
ENEKKAKELA AQRSQKQKEA KIAQEQSLKL SNMFNNMGKE GEQQVLKIIL KGDVQGSVEA
IRESLLKLST DEVKVDIIAS GIGAITSSDV TLAVASTAVV IGFNVRADSA AKKLAETDGV
EFRYYNIIYD LIDDVKKAMS GLLSPEMKEQ IIGIAEVREV YRSSKFGSIA GCMVIEGVVK
RTNPIRVLRN NVVIYEGTLE SLKRFKDDAS EVKKGLECGI GVKNYNDVRE GDQIEVFEVI
EVAKEL
