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IF2_STRPB
ID   IF2_STRPB               Reviewed;         953 AA.
AC   Q1JAC1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=MGAS2096_Spy1435;
OS   Streptococcus pyogenes serotype M12 (strain MGAS2096).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS2096;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000261; ABF36487.1; -; Genomic_DNA.
DR   RefSeq; WP_002983491.1; NC_008023.1.
DR   AlphaFoldDB; Q1JAC1; -.
DR   SMR; Q1JAC1; -.
DR   KEGG; spj:MGAS2096_Spy1435; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
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..953
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008349"
FT   DOMAIN          454..623
FT                   /note="tr-type G"
FT   REGION          48..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..470
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          488..492
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          509..512
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          563..566
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          599..601
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        52..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         463..470
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         509..513
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         563..566
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   953 AA;  105536 MW;  7B25E50A416483C6 CRC64;
     MSKKRLHEIA KEIGKSSKEV VEHAKYLGLD VKSHASSVEE ADAKKIISSF SKASKPDVTA
     SQTVKPKEVA QPSVTVVKET GSEHVEKTQV SKPKSRNFKA EREARAKEQA ARKQANGSSH
     RSQERRGGYR QPNNHQTNEQ GDKRITHRSQ GDTNDKRIER KASNVSPRHD NHQLVGDRNR
     SFAKENHKNG RFTNQKKQGR QEPQSKSPKI DFKARAAALK AEQNAEYSRQ SETRFRAQQE
     AKRLAELARQ EAKEAALKAQ AEEMSHREAA LKSIEEAETK LKSSNISAKS TADNRRKKQA
     RPEKNRELTH HSQEGQKKNK KSWNSQNQVR NQKNSNWNKN KKTKKGKNVK NTNTAPKPVT
     ERKFHELPKE FEYTEGMTVA EIAKRIKREP AEIVKKLFMM GVMATQNQSL DGDTIELLMV
     DYGIEAKAKV EVDDADIERF FEDENYLNPE NIVERAPVVT IMGHVDHGKT TLLDTLRNSR
     VATGEAGGIT QHIGAYQIEE AGKKITFLDT PGHAAFTSMR ARGASVTDIT ILIVAADDGV
     MPQTIEAINH SKAAGVPIIV AINKIDKPGA NPERVIAELA EYGIISTAWG GECEFVEISA
     KFNKNIDELL ETVLLVAEVE ELKADPTVRA IGTVIEARLD KGKGAIATLL VQQGTLHVQD
     PIVVGNTFGR VRAMVNDLGR RVKSAEPSTP VSITGLNETP MAGDHFAVYA DEKAARAAGE
     ERSKRALLKQ RQNTQRVSLD NLFDTLKAGE IKTVNVIIKA DVQGSVEALA ASLVKIEVEG
     VRVNVVHSAV GAINESDVTL AEASNAVIIG FNVRPTPQAR QQADTDDVEI RLHSIIYKVI
     EEVEEAMKGK LDPVYQEKIL GEAIIRETFK VSKVGTIGGF MVINGKVTRD SSVRVIRDSV
     VIFDGKLASL KHYKDDVKEV GNAQEGGLMI ENFNDLKVDD TIEAYIMEEI VRK
 
 
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