IF2_ACIAD
ID IF2_ACIAD Reviewed; 899 AA.
AC Q6FF40;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ACIAD0369;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67317.1; -; Genomic_DNA.
DR RefSeq; WP_004920460.1; NC_005966.1.
DR AlphaFoldDB; Q6FF40; -.
DR SMR; Q6FF40; -.
DR STRING; 62977.ACIAD0369; -.
DR PRIDE; Q6FF40; -.
DR EnsemblBacteria; CAG67317; CAG67317; ACIAD0369.
DR GeneID; 45232873; -.
DR KEGG; aci:ACIAD0369; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; ASP62977:ACIAD_RS01725-MON; -.
DR Proteomes; UP000000430; 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..899
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228160"
FT DOMAIN 399..568
FT /note="tr-type G"
FT REGION 94..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..415
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 433..437
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 508..511
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 544..546
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 899 AA; 98115 MW; DBCD22A53ED278A8 CRC64;
MTDKSIKELA LSVGRPVEKL LEQVREAGLP QRTANDIITT EQQDTLVNHL KKIHGQESGA
GKITLKRKTT STAKVASTSG KAKTINVEVR KKHTFTKPNP EQIAAEAKAR QETEERTRPQ
EQPRQAPQQQ MRDESENKAQ ATLNAMRAAQ QKETAKTTST TTEVVVKRKS TNKPIKPVNV
KQVETAEQRK AREAEAAKLK AVEETARRKA AEEAQQRTLE QMRKMASKYS TEETGATIRV
IDDSPLAAGL VGQAYEDSFN QEDREIKRGG ATNPRGQKKG GRNNQEEQSF KSHHKRGLKT
SQANKHGFEK PVKKQVYDVE IGSTIVVADL AQKMAIKVRE VIKTLMKMGE LVTQNQSIDQ
DTAALVVEEM GHNPILVSDT QAEDNLLEAA EEARGEQTTR PPVVTIMGHV DHGKTSLLDR
IRRSKVAAGE AGGITQHIGA YHVETDKGII TFLDTPGHAA FTAMRSRGAK ATDIVVLVVA
ADDGVMPQTA EAIDHARAAG TPIIVAINKM DKESADPDRV LNELTTKQIV PEQWGGDVPV
AMVSAHSGQG IDELLDLILI QSELMELKAS GEGAAQGVVI EARVDKGRGA VTSILVQNGT
LNIGDLVLAG SSYGRVRAMS DENGQPIKSA GPSIPVEILG LPDAPMAGDE VLVVNDEKKA
REVADARADR ERQKRIERQS AMRLENIMAS MGKKDVPTVN VVLKADVRGT LEALTAALNE
LSMDEVRVRV ISSGVGAITE SDVTLAESSE AVLLGFNVRA DTTARQKSDQ DGIDIRYYSI
IYELIDDVKN AMSGKLAPEH RETILGVAEV REVFHSSKFG AAAGCMVLEG MLHRNKPIRV
LRDDVVVFQG ELESLRRYKE VVEEVRAGME CGLAVKGYKD IKAKDKIEVY DVQLIKRSL
