ID   IF2_SALG2               Reviewed;         892 AA.
AC   B5REN6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SG3177;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR38976.1; -; Genomic_DNA.
DR   RefSeq; WP_000133061.1; NC_011274.1.
DR   AlphaFoldDB; B5REN6; -.
DR   SMR; B5REN6; -.
DR   EnsemblBacteria; CAR38976; CAR38976; SG3177.
DR   KEGG; seg:SG3177; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000008321; 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..892
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093820"
FT   DOMAIN          391..560
FT                   /note="tr-type G"
FT   REGION          93..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..407
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          425..429
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          446..449
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          500..503
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          536..538
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        93..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         400..407
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         446..450
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         500..503
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   892 AA;  97414 MW;  DD5BEA707A7E2D49 CRC64;
     MTDVTLKALA AERQVSVDRL VQQFADAGIR KSADDSVSAQ EKQTLLAHLN REAVSGPDKL
     TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR IFVKRDPQEA ERLAAEEQAQ REAEEQARRE
     AEEQAKREAQ QKAEREAAEQ AKREAAEKAK REAAEKDKVS NQQTDDMTKT AQAEKARREN
     EAAELKRKAE EEARRKLEEE ARRVAEEARR MAEENKWTAT PEPVEDTSDY HVTTSQHARQ
     AEDENDREVE GGRGRGRNAK AARPAKKGKH AESKADREEA RAAVRGGKGG KRKGSSLQQG
     FQKPAQAVNR DVVIGETITV GELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA
     EEMGHKVILR RENELEEAVM SDRDTGAAAE PRAPVVTIMG HVDHGKTSLL DYIRSTKVAS
     GEAGGITQHI GAYHVETDNG MITFLDTPGH AAFTSMRARG AQATDIVVLV VAADDGVMPQ
     TIEAIQHAKA AGVPVVVAVN KIDKPEADPD RVKNELSQYG ILPEEWGGES QFVHVSAKAG
     TGIDELLDAI LLQAEVLELK AVRKGMASGA VIESFLDKGR GPVATVLVRE GTLHKGDIVL
     CGFEYGRVRA MRNELGQEVL EAGPSIPVEI LGLSGVPAAG DEVTVVRDEK KAREVALYRQ
     GKFREVKLAR QQKSKLENMF ANMTEGEVHE VNIVLKADVQ GSVEAISDSL LKLSTDEVKV
     KIIGSGVGGI TETDATLAAA SNAILVGFNV RADASARKVI ESESLDLRYY SVIYNLIDEV
     KAAMSGMLSP ELKQQIIGLA EVRDVFKSPK FGAIAGCMVT EGTIKRHNPI RVLRDNVVIY
     EGELESLRRF KDDVNEVRNG MECGIGVKNY NDVRVGDMIE VFEIIEIQRT IA