IF2_STRPF
ID IF2_STRPF Reviewed; 953 AA.
AC Q1J5B4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=MGAS10750_Spy1522;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF38472.1; -; Genomic_DNA.
DR RefSeq; WP_011528896.1; NC_008024.1.
DR AlphaFoldDB; Q1J5B4; -.
DR SMR; Q1J5B4; -.
DR EnsemblBacteria; ABF38472; ABF38472; MGAS10750_Spy1522.
DR KEGG; spi:MGAS10750_Spy1522; -.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002434; 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..953
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008352"
FT DOMAIN 454..623
FT /note="tr-type G"
FT REGION 52..241
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..241
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; 105508 MW; 4C41EBD2515069EA CRC64;
MSKKRLHEIA KEIGKSSKEV VEHAKYLGLD VKSHASSVEE ADAKKIISSF SKASKPDVTA
SQTVKPKEVA QPSVTVVKET GSEHVEKTQV SKPKSRNFKA EREARAKEQA ARKQANGSSH
RSQERRGGYR QPNNHQTNEQ GDKRITHRSQ GDTNDKRIDR 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 GECEFVEISA
KFNKNIDELL ETVLLVAEVE ELKADPTVRA IGTVIEARLD KGKGAIATLL VQQGTLHVQD
PIVVGNTFGR VRAMVNDLGR RVKSAEPSTP VSITGLNETP MAGDHFAVYA DEKAARAAGE
ERSKRALLKQ RQNTQRVSLD NLFDTLKAGE IKTVNVIIKA DVQGSVEALA ASLVKIEVEG
VRVNVVHSAV GAINESDVTL AEASNAVIIG FNVRPTPQAR QQADTDDVEI RLHSIIYKVI
EEVEEAMKGK LDPVYQEKVL GEAIIRETFK VSKVGTIGGF MVINGKVTRD SSVRVIRDSV
VIFDGKLASL KHYKDDVKEV GNAQEGGLMI ENFNDLKVDD TIEAYIMEEI VRK
