ID   IF2_STRSV               Reviewed;         930 AA.
AC   A3CQ18;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SSA_1896;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45273.1; -; Genomic_DNA.
DR   RefSeq; WP_011837434.1; NC_009009.1.
DR   RefSeq; YP_001035823.1; NC_009009.1.
DR   AlphaFoldDB; A3CQ18; -.
DR   SMR; A3CQ18; -.
DR   STRING; 388919.SSA_1896; -.
DR   PRIDE; A3CQ18; -.
DR   EnsemblBacteria; ABN45273; ABN45273; SSA_1896.
DR   KEGG; ssa:SSA_1896; -.
DR   PATRIC; fig|388919.9.peg.1798; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002148; 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; 2.
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..930
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008355"
FT   DOMAIN          432..599
FT                   /note="tr-type G"
FT   REGION          27..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..448
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          466..470
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          487..490
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          541..544
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          577..579
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        27..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..265
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         441..448
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         487..491
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         541..544
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   930 AA;  102360 MW;  F8811B181BF9B926 CRC64;
     MSKVRLYEIA KELGKESKEV VARAKELGLD VKSHSSSVEA DAGERIKSSF TKAAAPQAPA
     EKPVAAQPSP QKTPAKEAAP VKAEPTEAKA AAQPEAKTET AAPVKRPQSR NFKAEREARA
     KEEAERRKQQ GNRKPQNKEQ GKREDRDNRN KNRGNSNDRD RGNRPNDRRD NRGQDGRRNG
     QNHQGFNGQK RQQPQGPKID FKARAAALKA EQNAEYARSS EERFKQAQEA KEVMERQNRR
     KEQPKAEAPA PVQPAPAPSA PAANPSPAPA AVDTRRKKQA RPDKKRDDFD REEEGPRKQQ
     KNRSSQNQVR NQRNSNWNKN KKNKKGKGNN NQAPKPVTER KFHELPTEFE YTDGMTVAEI
     AKRIKREPAE IVKKLFMMGV MATQNQSLDG DTIELLMVDY GIEAKKKVEV DTADIERFFV
     EEGYINQDAL VERPPVVTIM GHVDHGKTTL LDTLRNSRVA TGEAGGITQH IGAYQIEESG
     KKITFLDTPG HAAFTSMRAR GASVTDITIL VVAADDGVMP QTIEAINHSK AADVPIIVAI
     NKIDKPGANP ERVIGELAEH GVMSTAWGGD SEFVEISAKF NQNIDSLLET VLLVAEIQEL
     KADPTVRAIG TVIEARLDKG KGAVATLLVQ QGTLNVQDPI VVGNTFGRVR AMTNDLGRRV
     KVAGPSTPVS ITGLNETPMA GDHFAVYEDE KAARAAGEER AKRALLKQRQ ATHRVSLENL
     FDTLKAGEVK SVNVIIKADV QGSVEALSAS LQKIEVEGVK ITIVHSAVGA INESDVTLAE
     ASNAFIIGFN VRPTSQARQQ AEADDVEIRL HSIIYKVIEE MEDAMKGMLD PEYEEKIIGE
     ALIRETFKVS KVGTIGGFMV INGKVTRDSK VRVIRDGVVI YDGELASLKH FKDDVKEVTN
     GREGGLMIDG YNDIQVDDTI EAYIMEEIKK