ID   IF2_ACIAC               Reviewed;         943 AA.
AC   A1TSK3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Aave_3383;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000512; ABM33941.1; -; Genomic_DNA.
DR   RefSeq; WP_011796442.1; NC_008752.1.
DR   AlphaFoldDB; A1TSK3; -.
DR   SMR; A1TSK3; -.
DR   STRING; 397945.Aave_3383; -.
DR   PRIDE; A1TSK3; -.
DR   EnsemblBacteria; ABM33941; ABM33941; Aave_3383.
DR   KEGG; aav:Aave_3383; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002596; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..943
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335453"
FT   DOMAIN          443..612
FT                   /note="tr-type G"
FT   REGION          57..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..459
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          477..481
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          498..501
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          552..555
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          588..590
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        120..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         452..459
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         498..502
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         552..555
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   943 AA;  101154 MW;  9FAF19D383651E6B CRC64;
     MSSNTVAEFA SELKKSPETL LDQLKSAGVS KAAPSDALTE SDKQKLLAFL QASHGTATGD
     RRKITLTKKS TSEIKQADAT GKARTIQVEV RKKRTFIKRD DVVEGEGQGA APEVSAPSAE
     DQDLARREEE ARHQAELIRH QEEELSAARR EREERERRER EAEERAAAYA AQQAEKKAQE
     SAVREEASRE AAAEAAARAA AQAEARAKAE AESKARAAEE SARAADLDER RRKALAEAEA
     IRAMMAAPKK VLVAKKPEEP KPAAKPATAA DAKKGTLHKP AATPGARPAA GAPAGGGKEV
     KSAKLSSSWA GDPAKKKEIK TRGDASGGVG RNNWRSGPRG RRNDRDEQSH QQAAPVEARV
     IEVHVPETIT VAELAHKMSI KASEVIKSLM KMGQMVTINQ PLDQDTAMIV VEEMGHKAVV
     AALDDPEAFT DEDVSGQQAE ALPRAPVVTV MGHVDHGKTS LLDYIRRAKV AAGEAGGITQ
     HIGAYHVETP RGIVTFLDTP GHEAFTAMRA RGAQATDIVI LVVAADDGVM PQTKEAIKHA
     KAAGVPIVVA ITKADKPDAN PDRVKQELVA QEVVPEEYGG ESPFVPVSSK TGMGIDDLLE
     QVLLQAEVLE LKAPVEAMAK GLVIEAQLDK GRGPVATVLV QSGTLKVGDV VLAGQTSGRV
     RAMLDENGKA TKSAGPSIPV EIQGLSDVPQ AGDEFMVLSD ERRAREIATY RAGKFRNTKL
     AKQQAAKLEN VFADMTAGEV KNLPIIIKAD VQGSQEALAA SLLKLSTDEI RVQLVYAGVG
     GISESDVNLA IASKAIVIGF NVRADAGARK TAEANDVDLH YYNIIYDAVD ELKAAMSGML
     APEQREEEIG TAEIRTVFVA SKIGTVAGSY VTSGQVTRNC RFRLLRDNVV IYTGEVESVR
     RLKDDVKEVK EGFECGIKLK NYSDIKEGDQ LEFFEIKEIA RTL