IF2_FRATF
ID IF2_FRATF Reviewed; 846 AA.
AC A7NEI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FTA_1916;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU62391.1; -; Genomic_DNA.
DR RefSeq; WP_010032493.1; NC_009749.1.
DR AlphaFoldDB; A7NEI8; -.
DR SMR; A7NEI8; -.
DR KEGG; fta:FTA_1916; -.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OMA; NRDNRTG; -.
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_1000008244"
FT DOMAIN 345..512
FT /note="tr-type G"
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; 92343 MW; AE0605A57609D38B CRC64;
MAEITVGQLA QQTNKEVDAL LKQLKSFGIE KSSEKDTLTP TEMKTLLEKI NSAKNTATRK
KVTSVKLDGK HKINVSVKRK RRVAKKMEQQ ESTTLEQPQE LETMVQEVSQ QVDIVKEQDN
IEQIVENKEA VKVQEQRQAE IAKPVIKDSG FKITAMPEIK IEEIVAEDDE GLAASDKQAK
KKAAKKVFSE AVNTNTKYKC EEEEKKSKAK KAGGKGFKKA NPRQLSQLAG DLESFDEFGA
KKGKLKAPKV KKQEFTKPVE NTVRTVEIHE GITVSELAQK MAVKGAEIVK VLFNMGVMAT
INQSLDQDTA ILIVEEMGHK YTLHNENALE EAVTIVDRSS YKKISRAPVV TIMGHVDHGK
TSLLDYIRQT RVVAGEAGGI TQHIGAYSVK TDKGSITFLD TPGHEAFTSM RARGAKSTDI
VILVVAADDG VMPQTEEAIQ HAKAARVPIV VAVNKIDKPE ADSDKVISEL 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