IF2_BUCAI
ID IF2_BUCAI Reviewed; 864 AA.
AC P57458;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=BU377;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000003; BAB13081.1; -; Genomic_DNA.
DR RefSeq; NP_240195.1; NC_002528.1.
DR RefSeq; WP_009874335.1; NC_002528.1.
DR AlphaFoldDB; P57458; -.
DR SMR; P57458; -.
DR STRING; 107806.10039047; -.
DR EnsemblBacteria; BAB13081; BAB13081; BAB13081.
DR KEGG; buc:BU377; -.
DR PATRIC; fig|107806.10.peg.391; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; VIFAMNK; -.
DR Proteomes; UP000001806; 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; Reference proteome.
FT CHAIN 1..864
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137180"
FT DOMAIN 364..533
FT /note="tr-type G"
FT REGION 140..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..380
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 398..402
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 419..422
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 473..476
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 509..511
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 373..380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 419..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 473..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 864 AA; 97518 MW; 55031AFEBCDC9F3C CRC64;
MPDISLKVLS NEIKISIQEL IKELSIIGIT KTEDNYINVL EKNILLKHLE SKKKYSLDTL
VLQRKTRSTL RISTVGGKNK SVQVEVRKKR AYVKNNKFEN ESFLNEKKVI KHSMQKTSSL
KNKEKKYIKN IEKIELNKSD SRSLNTKKEN KLKISNKDEQ NKKFNQHRES NSFDLNHKKR
IKENKDIRIS HKEEKQDYHL TTFLHARQAE DENDREVEID KRNHGRILKN YRQKKNNKNF
HNGRYNKEEI RTFNRNKKNS KQKNKPILLQ QVFQKPESII NRDVIISNTI TVSDLANKMA
IKSSEVIKNM MNMGIIGTIN HVLDQDTAQL IAEEMGHKVI VHRENALEEL IMKDRDTGND
VSAIRAPVVT IMGHVDHGKT SLLDYIRSTK TAFYEAGGIT QNIGAYHVKT DLGSITFLDT
PGHSAFTAMR SRGVQITDIV ILVVAADDGV MPQTIEAIQH AKEANVPVIV AINKIDKTDS
DIDKVRNDLM KYNILSEEWG GENIFVSVSA KTGKGINKLL NVILLQAEML ELKAVTTGMA
EGIVVESFLD KGRGPIATVL VKKGQLKKGD VILCGFEYGR IKSLRDASGN EVFSAGPSIP
VEVLGLSKVP FSGDVVTVVR DEKKAREVAS YRKEKSREKK LSNQNRINLE NMFDDINKNN
VSELKIILKS DIQGSLEAIS GALLKLSTEE VKIKIIGLGI GGITETDASL ALASNAIILG
FNVRADTSAK KIINSEHLDL RYYSVIYDLL DEVKAAMTGL LSPEYKENII GLAEVRNTFK
SPKFGLIAGC MVTEGVIKRS NPIHILRNNI VIYEGELESL RRFKEDVNEI RNGLECGIGI
KNYNDIRVGD IIEVFEVREM KRIL