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IF2_STRP2
ID   IF2_STRP2               Reviewed;         930 AA.
AC   Q04LW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SPD_0482;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(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; CP000410; ABJ54884.1; -; Genomic_DNA.
DR   RefSeq; WP_000039219.1; NC_008533.2.
DR   AlphaFoldDB; Q04LW0; -.
DR   SMR; Q04LW0; -.
DR   STRING; 373153.SPD_0482; -.
DR   EnsemblBacteria; ABJ54884; ABJ54884; SPD_0482.
DR   GeneID; 60233978; -.
DR   KEGG; spd:SPD_0482; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   BioCyc; SPNE373153:G1G6V-531-MON; -.
DR   Proteomes; UP000001452; 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.
FT   CHAIN           1..930
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008348"
FT   DOMAIN          432..599
FT                   /note="tr-type G"
FT   REGION          50..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..346
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        64..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..333
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;  102937 MW;  1FD34F4AF9EE4115 CRC64;
     MSKKRLYEIA KELGKESKEV VARAKELGLD VKSHSSSVEE AVAAKIAASF KPAAAPKVEA
     KPAAPKVSAE KKTEKSEPAK PAVAKEEAKP AEPVAPKTEK VAAKPQSRNF KAEREARAKE
     QAERRKQNKG NNRDQQQNGN RQKNDGRNGG KQGQSNRDNR RFNDQAKKQQ GQQKRRNERR
     QQEDKRSNQA APRIDFKARA AALKAEQNAE YARSSEERFK QYQAAKEALA QANKRKEPEE
     IFEEAAKLAE QAQQVQAVVE VVPEKKEPAV DTRRKKQARP DKNRDDYDHE EDGPRKQQKN
     RSSQNQVRNQ KNSNWNNNKK NKKGNNKNNR NQTPKPVTER KFHELPTEFE YTDGMTVAEI
     AKRIKREPAE IVKKLFMMGV MATQNQSLDG ETIELLMVDY GIEAKQKVEV DNADIERFFV
     EDGYLNEDEL VERPPVVTIM GHVDHGKTTL LDTLRNSRVA TGEAGGITQH IGAYQIVENG
     KKITFLDTPG HAAFTSMRAR GASVTDITIL VVAADDGVMP QTIEAINHSK AANVPIIVAI
     NKIDKPGANP ERVIGELAEH GVMSTAWGGD SEFVEISAKF NQNIEELLET VLLVAEIQEL
     KADPTVRAIG TVIEARLDKG KGAVATLLVQ QGTLNVQDPI VVGNTFGRVR AMTNDLGRRV
     KVAGPSTPVS ITGLNEAPMA GDHFAVYEDE KSARAAGEER AKRALMKQRQ ATQRVSLENL
     FDTLKAGELK SVNVIIKADV QGSVEALSAS LQKIDVEGVK VTIVHSAVGA INESDVTLAE
     ASNAFIVGFN VRPTPQARQQ AEADDVEIRL HSIIYKVIEE MEEAMKGMLD PEFEEKVIGE
     AVIRETFKVS KVGTIGGFMV INGKVARDSK VRVIRDGVVI YDGELASLKH YKDDVKEVTN
     GREGGLMIDG YNDIKMDDVI EAYVMEEIKR
 
 
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