IF2_STRP8
ID IF2_STRP8 Reviewed; 953 AA.
AC Q8NZU7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=spyM18_1729;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL98258.1; -; Genomic_DNA.
DR RefSeq; WP_011018100.1; NC_003485.1.
DR AlphaFoldDB; Q8NZU7; -.
DR SMR; Q8NZU7; -.
DR KEGG; spm:spyM18_1729; -.
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_0000137268"
FT DOMAIN 454..623
FT /note="tr-type G"
FT REGION 48..248
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 227..248
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; 105464 MW; 6D9C4630592B80EE CRC64;
MSKKRLHEIA KEIGKSSKEV VEHAKYLGLD VKSHASSVEE ADAKKIISSF SKASKPDVTA
SQTVKPKEVA QPSVTVVKET GSEHAEKTQV 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 GDSEFVEISA
KFNKNIDELL ETVLLVAEVE ELKADPTVRA IGTVIEARLD KGKGAIATLL VQQGTLHVQD
PIVVGNTFGR VRAMVNDLGR RVKSAEPSTP VSITGLNETP MAGDHFAVYA DEKAARAAGE
ERSKRALLKQ RQNTQRVSLD NLFDTLKAGE IKTVNVIIKA DVQGSVEALA ASLVKIDVEG
VRVNVVHSAV GAINESDVTL AEASNAVIIG FNVRPTPQAR QQADTDDVEI RLHSIIYKVI
EEVEEAMKGK LDPVYQEKIL GEAIIRETFK VSKVGTIGGF MVINGKVTRD SSVRVIRDSV
VIFDGKLASL KHYKDDVKEV GNAQEGGLMI ENFNDLKVDD TIEAYIMEEI VRK
