IF2_BUCBP
ID IF2_BUCBP Reviewed; 876 AA.
AC Q89AF5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=bbp_340;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27061.1; -; Genomic_DNA.
DR RefSeq; WP_011091462.1; NC_004545.1.
DR AlphaFoldDB; Q89AF5; -.
DR SMR; Q89AF5; -.
DR STRING; 224915.bbp_340; -.
DR PRIDE; Q89AF5; -.
DR EnsemblBacteria; AAO27061; AAO27061; bbp_340.
DR GeneID; 56470879; -.
DR KEGG; bab:bbp_340; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000601; 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..876
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137182"
FT DOMAIN 378..547
FT /note="tr-type G"
FT REGION 387..394
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 412..416
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 433..436
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 487..490
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 523..525
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 387..394
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 433..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 487..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 876 AA; 99065 MW; 8E4790E6B8BA5D0E CRC64;
MEMINIQDLA NEVDMSVDRL VQVCIKIGIL KTKYDTITQL EKLTILNYLN ENLKNSNKNV
LMLKRKIRST VKIFSSGGKN KCISIEIRKN KRYSKSNDDI KTFLEKNKDI NLNKSEIVLS
AKEDSKIFVS HSKDNINSNI NDTCTIRKKF NKNFKKQQKI NILSEKEDKN NLDNVLNVEQ
GSKKKINFKN VVLEEKKENK VKFSNYIKLS EKYNTRKVSN FLTSKNIRDH NNVEKHRRNR
NKILRNKHQK DNFSFEKNLS DKNIKLDNCI HKKSIKNKKE SLLKQVFKKP LRAINRNIIL
SSAISIFNLA NKMAVKSSEI IKMMARLGYT VTINQIIDQD IAQLVAEEMG HKVTICYENK
LEDKIMRDRD FGDGIKKTRP PIITIMGHVD HGKTSLLDKI RLTRVADSEP GRITQHIGAY
HIKINNKIIT FLDTPGHSAF TAMRARGAQV TDIVILVIAI DDGIKPQTIE AIQHAQAASV
PIIIAINKID KLITNIEKIK NELTKYNILP EEWGGDNIFV NISAKSGEGI ESLLNAILTQ
SEMLELKSIS NGMASGLVIE SYLDKGRGPT AIILIKEGKL NKGDIVLCGF EYGKVRSIRD
DLENEVNSIG PSIPVKILGL SGIPLAGDKI VVVRDEKQAR EVATYRQKKF KEQKMSKQRQ
LKSLDIFEDV KRSSNPSLNI VIKSDVQGSL EAISYSLLKL SNDEIKINII GKGVGGITET
DVLLAAASNA IIIGFNVRAD SSAKRIIEFE NVDFRYYSVI YQIIDEIKNC ICGMLSPKYQ
QKIIGLANVR SIFKSPKIGV IAGCIVMEGI IKRNSIIQIL RNNVVIHKGE LISLRRFKED
VSEVRCGVEC GIGMKNFNDI CIEDIIEVFE TIEIKQ
