IF2_STRE4
ID IF2_STRE4 Reviewed; 956 AA.
AC C0M8P7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SEQ_0518;
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047;
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; FM204883; CAW92747.1; -; Genomic_DNA.
DR RefSeq; WP_012679100.1; NC_012471.1.
DR AlphaFoldDB; C0M8P7; -.
DR SMR; C0M8P7; -.
DR PRIDE; C0M8P7; -.
DR EnsemblBacteria; CAW92747; CAW92747; SEQ_0518.
DR KEGG; seu:SEQ_0518; -.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001365; 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..956
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190634"
FT DOMAIN 457..626
FT /note="tr-type G"
FT REGION 33..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..473
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 491..495
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 512..515
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 566..569
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 602..604
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..210
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..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 512..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 566..569
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 956 AA; 104910 MW; 1A91EF8A92641291 CRC64;
MSKKRLHEIA KEIGKSSKEV VERAKSLGLD VKSHASSVEE ADANKIASSF SAGVTKNVQA
GSAKDKQVAE QKAKAAKATT PQPAASKAAE KPAAATQEAS QPVAVKPKSR NFKAEREARA
KEQVARRQAG QNRSNDRKSD YRQLGRSQGQ QTERAGHKSQ NQQRDRRFDN RPSSGNNRND
GHRQAGNRDK NRSFNANSRQ QDTGRQGQTQ AGAPKIDFKA RAAALKAEQN AEYARQRESR
FREQEEAKRL EQQARQEAKA AALKAQTEDK KHREASAKAT ESVASMAAAS VAKPVDKRRK
KQNRPDKGHD RDHGLEDGQK KNKKSWNSQN QVRNQKNSNW NNNKKNKKGK HHKNSNTAPK
PVTERKFHEL PKEFEYSEGM TVAEIAKRIK REPAEIVKKL FMMGVMATQN QSLDGDTIEL
LMVDYGIEAK AKVEVDEADI ERFFTDDSYL NPENIVERAP VVTIMGHVDH GKTTLLDTLR
NSRVATGEAG GITQHIGAYQ IEEAGKKITF LDTPGHAAFT SMRARGASVT DITILIVAAD
DGVMPQTIEA INHSKAAGVP IIVAINKIDK PGANPERVIS ELAEHGIIST AWGGECEFVE
ISAKFNKNID ELLETVLLVA EVEELKADPT VRAIGTVIEA RLDKGKGAVA TLLVQQGTLH
VQDPIVVGNT FGRVRAMTND LGRRVKSAEP STPVSITGLN ETPMAGDHFA VYADEKAARA
AGEERAKRAL LKQRQNTQRV SLDNLFDTLK AGEIKTVNVI IKADVQGSVE ALAASLLKID
VEGVRVNVVH SAVGAINESD VTLAEASNAV IIGFNVRPTP QARQQADTDD VEIRLHSIIY
KVIEEVEEAM KGKLDPEYQE KMLGEAIIRE TFKVSKVGTI GGFMVVNGKV TRDSSVRVIR
DSVVIFDGKL ASLKHYKDDV KEIGNAQEGG LMIEGFNDIK VDDTIEAYVM EEITRK
