IF2_BUCAP
ID IF2_BUCAP Reviewed; 867 AA.
AC Q8K9H1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BUsg_365;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67918.1; -; Genomic_DNA.
DR RefSeq; WP_011053885.1; NC_004061.1.
DR AlphaFoldDB; Q8K9H1; -.
DR SMR; Q8K9H1; -.
DR STRING; 198804.BUsg_365; -.
DR PRIDE; Q8K9H1; -.
DR EnsemblBacteria; AAM67918; AAM67918; BUsg_365.
DR KEGG; bas:BUsg_365; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000416; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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..867
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137181"
FT DOMAIN 367..534
FT /note="tr-type G"
FT REGION 376..383
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 401..405
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 422..425
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 476..479
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 512..514
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 376..383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 422..426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 476..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 867 AA; 97701 MW; B07453E3AA276920 CRC64;
MVDISLKILS NEMKISIKEL IKTLSEISIS KTENDCISIT EKKNLLKYLE SKKKPFLNTF
ILQRKTRSTL NVFTPGGKNK SVQIEIRKKR MYLKNNKSEL EPLLKNKNLL QNKEKNNLKS
LKNTISKAKE SQKNIDILEE SKANINFKNL NKLTKSNVFN KNEKNKSLKK NINFNNHSFY
SKKTIKNNTE NQKLYKEEKK DYHLTTFIHN RNTEDNRDRE IEKNKRNFHR NIKNYRQKKN
NKQNNQIKSK KDEVRISKNR KNVKQKNKSI LLQQVFKKPE SVINRDVVIN GAITVCDLAN
KMAIKSSEVI KNMMNMGIIG TINHVLDQDT AQLIAEEMGH KVILRRENEL EELIMKDRDT
GNNISLTRAP VVTIMGHVDH GKTSLLDYIR STKVASSEAG GITQNIGAYH VTTDFGSVTF
LDTPGHSAFT GMRSRGVKIT DIVVLVVAAD DGVKPQTIEA IQHAKEANVP IIVAINKIDK
VDSNIDQIKN DLTKYNILSE EWGGENIFVL ISAKTGKGID NLLNAILLQS EILELKAIST
GMAEGVVIES FLDKGRGPIA TVLVQKGNLK KGDIILCGFE YGRIKVLRNE NGKTLKHAGP
SMPVEVLGLS KVPFSGEKVT VVRDEKKAKE VASYRKNKSR EIKLANQNRS SLENMFKNIK
KNDFSELKII IKSDVQGSLE AISSALFKLS TNEVKVNIIG SGIGGITETD ASLALASNAI
ILGFNVRADA SAKKIIDLEN LDLRYYSVIY DLLNEVKAAM TGLLSPQYKQ NIIGLAEVRN
IFKSPKFGLI AGCMVTEGII KRNNPIRILR NNVVVYEGEL ESLRRFKEDI NEIRNGMECG
IGIKNYHDLN IGDVIEVFEV KEIKRIL
