ID   IF2_PETMO               Reviewed;         700 AA.
AC   A9BJ54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pmob_0255;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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; CP000879; ABX30999.1; -; Genomic_DNA.
DR   RefSeq; WP_012208106.1; NC_010003.1.
DR   AlphaFoldDB; A9BJ54; -.
DR   SMR; A9BJ54; -.
DR   STRING; 403833.Pmob_0255; -.
DR   EnsemblBacteria; ABX30999; ABX30999; Pmob_0255.
DR   KEGG; pmo:Pmob_0255; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000789; 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; 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; PF04760; IF2_N; 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.
FT   CHAIN           1..700
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075612"
FT   DOMAIN          191..365
FT                   /note="tr-type G"
FT   REGION          58..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..207
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          225..229
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          246..249
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          300..303
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          337..339
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..207
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         246..250
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         300..303
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   700 AA;  78579 MW;  0677DEEB6734F838 CRC64;
     MSKTRIYEVA KELGMNSKEL MEFLEKELNI SVKSHMSTIE EETVQVIMDL IEEERQTKKE
     VKKQKEPSKE KGKSSEQVKV KEKSKEEPVE EKFLREVTIT SHDLSLDILA KQIGLEQNDI
     IKDMFMKGVV LRPGQKLDIT MAENIAMNYN VILNFEIEKK ETEEGKEQDI EAILAKKWND
     IYEKEKDKLA PRPPVVTIMG HVDHGKTTLL DKIRNTHVAD KEEGGITQSI GAYQIEYNGQ
     KITFIDTPGH EAFTEMRARG AQVTDIVVLI IAADDGVMPQ TIEAYNHAKS ANVPIIVAIN
     KIDKPNANVE LTKQQMVSKL NLIPEDWGGD TITVLVSAKT GEGIDELLEM ILLVSEMQEI
     RCIPDGKARA VIIESRVDKA MGPLGTVIVK DGILKVGDDF ISGSTYGRVR RLINDKGESL
     IKAVPSTPVQ VLGFNDVPNT HSILYVIDSK EEARTLAEKV KEKEEEKSKG PAKRHVKLED
     IMQKMEEEEK KKLNILLKAS TYGEIEALRN AIQKFENPEI DIEIIHAGIG PVSTSDIMLA
     SASDAIVLGF RVKADSKALK MAEAEGIEVR RYNIIFDLID DIKKALEGML EPIQKEELTG
     NGVIKEEFKI KGVGKIAGVQ VNEGYVQRDG GVRIYRNGGL IADVKIKSLK HYKDEVKSIE
     APKECGIQFE NFEDFTKGDE LEFYKHVFVK RELGLEQKTK