ID IF2_RICBR Reviewed; 828 AA.
AC Q1RIX0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RBE_0613;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04694.1; -; Genomic_DNA.
DR RefSeq; WP_011477282.1; NC_007940.1.
DR AlphaFoldDB; Q1RIX0; -.
DR SMR; Q1RIX0; -.
DR KEGG; rbe:RBE_0613; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000001951; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Reference proteome.
FT CHAIN 1..828
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000277907"
FT DOMAIN 326..496
FT /note="tr-type G"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..342
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 360..364
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 382..385
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 472..474
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 382..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 828 AA; 90819 MW; ECB1BA5DDEA98915 CRC64;
MTDNQENKPK KLTLSNTKLS LNKSFDSLAS TQSFVNAKSK TLVEVRKSYS GSTTTLSLNK
EKGSLETGSS SGSEEFNRRL SILKKAAEQS KLNDNSQIST LSKLASINQS IASQEDPIEV
EQEESSDTNK VKEEPKIEEV KDIEESTLQT PKKKEDIFVK SPLVGTRTRY GIESEKTVDK
VTENKVIAPK PKVEESRKFK KTDLFNMVGD DENDNRNRTR SLASIKRARE KEKRKSLVQA
PEKVYREITL PEVIGVGDFA NAMSERVSDV IKELMKLGIL ANASQTIDAD TAELVATHLG
HAVKRVQESD VENILITNDK EEDLRSRAPV VTVMGHVDHG KTSLLDALKS TDVASGETGG
ITQHIGAYRV TLADGRAITF IDTPGHEAFS EMRSRGAGVT DIVIIVVAAD DGIKPQTVEA
INHAKAANVP IIVAINKIDK PDIDIERVKN ELYMYEIIGE EAGGDVMVIP ISALKKINLD
KLEEAILLIA EMQNLKASPF GSASGVVIES KIEKGRGALT TMLVQRGTLK SGDIIIAGTA
YGKVKKMTND KGIEVLEATP SVPIEIQGLS HVPHAGDMFN VVQTEKQAKD IAEYRERVAK
EKKISIAPRS SLEDLFLKAS GSSKIKELPL IIKGDVHGSV EAIAGSLLKL PNDEVKLRIL
HSGVGPITES DVSLAHASSA IIVGFNVRAG ANAKTAAEKE KVEIRYYSII YDLLDDVKAI
MSGMLDPIIR EQYIGSVEIR QIFNITKIGK IAGSYVTRGI IKKGAGVRLL RDNIVIHEGK
LKTLKRFKEE VKEVREGYEC GIAFENYEDI REGDTVEVFE LIQEKKQL
//
