IF2_STRS7
ID IF2_STRS7 Reviewed; 959 AA.
AC C0MDY5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SZO_15380;
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAX00225.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MDY5; -.
DR SMR; C0MDY5; -.
DR EnsemblBacteria; CAX00225; CAX00225; SZO_15380.
DR KEGG; seq:SZO_15380; -.
DR PATRIC; fig|40041.11.peg.1651; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; CHICSIW; -.
DR Proteomes; UP000001368; 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..959
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202784"
FT DOMAIN 460..629
FT /note="tr-type G"
FT REGION 33..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..476
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 494..498
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 515..518
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 569..572
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 605..607
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 42..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 515..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 569..572
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 959 AA; 105257 MW; BF288C487A7F95B2 CRC64;
MSKKRLHEIA KEIGKSSKEV VERAKSLGLD VKSHASSVEE ADANKIASSF SAGVTKNVQA
GSAKDKQVAE QKAKAAKATT PQPAASKAAE KPAAATQEAS QPVAVKPKSR NFKAEREARA
KEQVARRQAG QNRSNDRKSD YRQLGRSQGQ QTERAGHKSQ NQQRDRRFDN RPSSGNNRND
GHRQAGNRDK NRSFNANSRQ QDIGRQGQTQ AGAPKIDFKA RAAALKAEQN AEYARQRESR
FREQEEAKRL EQQARQEAKA AALKAQTEDK KHREAPAKAT EPAEPVASMA AAPVAKPVDK
RRKKQNRPDK AHDRDHGLED GQKKNKKSWN SQNQVRNQKN SNWNNNKKNK KGKHHKNSNT
APKPVTERKF HELPKEFEYS EGMTVAEIAK RIKREPAEIV KKLFMMGVMA TQNQSLDGDT
IELLMVDYGI EAKAKVEVDE ADIERFFTDD NYLNPDNIVE RAPVVTIMGH VDHGKTTLLD
TLRNSRVATG EAGGITQHIG AYQIEEAGKK ITFLDTPGHA AFTSMRARGA SVTDITILIV
AADDGVMPQT IEAINHSKAA GVPIIVAINK IDKPGANPER VISELAEHGI ISTTWGGECE
FVEISAKFNK NIDELLETVL LVAEVEELKA DPTVRAIGTV IEARLDKGKG AVATLLVQQG
TLHVQDPIVV GNTFGRVRAM TNDLGRRVKS AEPSTPVSIT GLNETPMAGD HFAVYADEKA
ARAAGEERAK RALLKQRQNT QRVSLDNLFD TLKAGEIKTV NVIIKADVQG SVEALAASLL
KIDVEGVRVN VVHSAVGAIN ESDVTLAEAS NAVIIGFNVR PTPQARQQAD ADDVEIRLHS
IIYKVIEEVE EAMKGKLDPE YQEKVLGEAI IRETFKVSKV GTIGGFMVVN GKVTRDSSVR
VIRDSVVIFD GKLASLKHYK DDVKEIGNAQ EGGLMIEGFN DIKVDDTIEA YVMEEIIRK
