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IF2_STRSY
ID   IF2_STRSY               Reviewed;         940 AA.
AC   A4VXH3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SSU05_1846;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(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; CP000407; ABP90812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VXH3; -.
DR   SMR; A4VXH3; -.
DR   STRING; 391295.SSU05_1846; -.
DR   PRIDE; A4VXH3; -.
DR   EnsemblBacteria; ABP90812; ABP90812; SSU05_1846.
DR   KEGG; ssu:SSU05_1846; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000243; 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..940
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008356"
FT   DOMAIN          442..609
FT                   /note="tr-type G"
FT   REGION          48..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..458
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          476..480
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          497..500
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          551..554
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          587..589
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        61..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         451..458
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         497..501
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         551..554
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   940 AA;  104075 MW;  7C3A9FEDECF27AB2 CRC64;
     MSKKRLNEIA RELGVSSKEV VAKAQELGFE VKSHASSVDE ASAKRLAESF GGQKSEATKV
     AAKVSKPEKV DETPKVETAK VEKAKETQPV VKEEVAASAV QSASHRPQSR NFKAEREARA
     KEQAAKRAQN QGKGGQAKSD QDRRDNRQLG QGRSNNERND RRDNRRDQRP EERKDNRFGD
     RRDNRDNRRQ DNRSGRLARF EQREAAKPAG PKIDFKARAA ALKAEQNAEY ARTSEERFRQ
     AQEAKKQPKK PKEIKFEEPV VESKPFVKPA LVASVPEQVA ETTVDTRRKK QARPDKKRDF
     NSDEEDGPRK QQRNRNSQNQ VRNQRTSNWN NNKKNKKGKA NQPAKPVTER KFHELPTEFE
     YTAGMTVAEI AKRIKREPAE IVKKLFLMGV MATQNQSLDG DTIELLMVDY GIEAKEKVEV
     DNADIERFFV EEGYLNEEEM TERPPVVTIM GHVDHGKTTL LDTLRNSRVA TGEAGGITQH
     IGAYQIEEAG KKITFLDTPG HAAFTSMRAR GASVTDLTIL VVAADDGVMP QTIEAINHSK
     AANVPIIVAI NKIDKPGANP ERVIGELAEH GVISTAWGGE SEFVEISAKF NQNIDELLET
     VLLVAEIQEL KADPTVRAIG TVIEAHLDKG KGAVATLLVQ QGTLNVQDPI VVGNTFGRVR
     AMTNDLGRRV KTAGPSTPVS ITGLNETPMA GDHFAVYEDE KSARAAGEER AKRALLKQRQ
     ATQRVSLENL FDTLKAGEVK SVNVIIKADV QGSVEALASS LQKIEVEGVR VNIVHSAVGA
     INESDITLAE ASNALVIGFN VRPTAEARSQ AEADDVEVRL HSIIYKVIEE MEDAMKGMLD
     PEYEEKIIGE AIIRETFKVS KVGTIGGFMV VRGKVTRDSS VRVIRDGVVV FDGKLASLKR
     YKDDVKEVGN AQEGGLMIEN YNDLKVDDTI EAYIMEEIKK
 
 
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