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
