IF2_AZOVD
ID IF2_AZOVD Reviewed; 836 AA.
AC C1DFK9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Avin_42820;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO80405.1; -; Genomic_DNA.
DR RefSeq; WP_012702773.1; NC_012560.1.
DR AlphaFoldDB; C1DFK9; -.
DR SMR; C1DFK9; -.
DR STRING; 322710.Avin_42820; -.
DR PRIDE; C1DFK9; -.
DR EnsemblBacteria; ACO80405; ACO80405; Avin_42820.
DR KEGG; avn:Avin_42820; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002424; 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; 2.
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..836
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202763"
FT DOMAIN 336..505
FT /note="tr-type G"
FT REGION 114..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..352
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 370..374
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 391..394
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 481..483
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 114..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 391..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 836 AA; 90863 MW; DB5BC74AAEC74F24 CRC64;
MTQVTVKELA LVVDTPVERL LQQMREAGLS HTSAEQVVTD NEKQALLAHL KGSHGVKLEE
PRKITLQRKT TTTLRVAGSK TISVEVRKKK TYVKRSPDEL EAEKQRELEE QRAAEEAAVR
QKAGEEARRR AAEQEAQRQA EAAAAAAVAA KEPESALGVA PEPVAAPPAS EERKREEPRR
VDKEKVRNVD DERRERKNAQ HRPSIKDKAP AARAVVRSVD EDGEGFGRRG GRGGKSKLKK
RNQHGFQNPT GPVVREVTIG ETITVAELAQ QMSVKAAEVI KFMFKMGTPV TINQVLDQET
AQLLAEELGH KVKLVSENAL EEQLAESLKF EGEAEARAPV VTVMGHVDHG KTSLLDYIRR
TKVATGEAGG ITQHIGAYHV ETDRGMITFL DTPGHAAFTA MRARGAKATD IVILVVAADD
GVMPQTEEAI QHAKAAGVPI VVAVNKIDKP EADPDRVKND LAARDVIPEE WGGDTQFVHV
SAKAGTGIDE LLEAVLLQAE VLELKATPSA PGRGVVIESR LDKGRGPVAT VLVQNGTLRQ
GDVVLAGVNF GRVRAMLDEN GQPLKEAGPS IPVEILGLDS TPDAGDELTV VTDEKKAREV
ALFRQGKFRE VKLARQHSAK LENIFETMGQ DEKKTLNIVL KADVRGSLEA LQGALSELGN
EEVQVRVVGG GVGGITESDA NLALASNAVL FGFNVRADAG ARKIVEQEGL DLRYYNVIYD
IIEDVKKALS GMLGSEVREN ILGVAEVRDV FRSPKFGAIA GCMVLEGNVH RNRPIRVLRD
DVVIFEGELE SLRRFKDDVS EVRAGMECGI GVKSYNDVKV GDKIEVYEKV QVARSL
