ID IF2_FRATH Reviewed; 846 AA.
AC Q2A1G8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FTL_1809;
OS Francisella tularensis subsp. holarctica (strain LVS).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=376619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVS;
RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA Garcia E.;
RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT Strain).";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AM233362; CAJ80248.1; -; Genomic_DNA.
DR RefSeq; WP_011457537.1; NZ_CP009694.1.
DR AlphaFoldDB; Q2A1G8; -.
DR SMR; Q2A1G8; -.
DR KEGG; ftl:FTL_1809; -.
DR Proteomes; UP000001944; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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_1000008245"
FT DOMAIN 345..512
FT /note="tr-type G"
FT REGION 199..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; 92422 MW; 003F0A4E74351AF6 CRC64;
MAEITVGQLA QQTNKEVDAL LKQLKSFGIE KSSEKDTLTP TEMKTLLEKI NSAKNTATRK
KVTSVKLDGK HKINVSVKRK RRVAKKMEQQ ESTTLEQPQE LETMVQEVSQ QVDIVKEQDN
IEQIVENKEA VKVQEQRQAE IAKPVIKDSG FKITAMPEIK IEEIVAEDDE GLAASDKQAK
KKAAKKVFSE AVNTNTKYKR EEEEKKSKAK KAGGKGFKKA NPRQLSQLAG DLESFDEFGA
KKGKLKAPKV KKQEFTKPVE NTVRTVEIYE 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
//
