ID   IF2_STRT2               Reviewed;         943 AA.
AC   Q5M5V5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=stu0344;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60064.1; -; Genomic_DNA.
DR   RefSeq; WP_011225498.1; NC_006448.1.
DR   AlphaFoldDB; Q5M5V5; -.
DR   SMR; Q5M5V5; -.
DR   STRING; 264199.stu0344; -.
DR   EnsemblBacteria; AAV60064; AAV60064; stu0344.
DR   KEGG; stl:stu0344; -.
DR   PATRIC; fig|264199.4.peg.350; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001170; 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..943
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228250"
FT   DOMAIN          445..614
FT                   /note="tr-type G"
FT   REGION          30..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..461
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          479..483
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          500..503
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          554..557
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          590..592
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        30..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         454..461
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         500..504
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         554..557
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   943 AA;  103880 MW;  4A24BE3E77D3D1BA CRC64;
     MSKKRLYEIA KEVGVESKVI VAKAQELGLS VKSHSSSVEE ADANRITSSL KPGTAKDESK
     PAPKATPTPK EEKVEPKVDK ASVAKSAPAK ETSKAEVKEA SVALKKPKSR NFKAEREARA
     KAEAERRKNG GGRDNRNRNQ QGNDQGKRHN NDRRNQKGNG QGDHNKGNRD NSTNHDRNFQ
     GKLRNDQNQN NRRDNARNNQ AGPRIDLKAR AAALKAEQNA EYSRQSETRF REEKAAEQRR
     AKEQEKARKE KQQVKVAVQK AAAETKPAPK PAPVAPQSAP TAQVQDTRRK KVRPNKSRDN
     RRVNEDGPKQ TRNNKWNNQN QVRNQRNSNW NKNKNKKGKN NRGNSAPKPV TERKFHELPK
     EFEYTEGMTV AEIAKRIKRE PAEIVKKLFM MGVMATQNQS LDGDTIELLM VDYGIEATKK
     EEVDNADIER FFVDEDYLNK DAMVERAPVV TIMGHVDHGK TTLLDTLRNS RVATGEAGGI
     TQHIGAYQIE EGGKKITFLD TPGHAAFTSM RARGASVTDI TVLIVAADDG VMPQTIEAIN
     HSKAAGVPII VAINKIDKPD ANPERVIGEL AEHGVISTAW GGDSEFVEIS AKFGQNIEEL
     LETILLVAEV EELKADPTVR AIGTVIEARL DKGKGAVATL LVQQGTLNVQ DPIVVGNTFG
     RVRAMTNDLG RRIKTAGPSA PVSITGLNEA PMAGDHFAVY EDEKAARAAG EERAKRALMK
     QRQQTHRVSL DNLFDTLKAG EMKTVNVIIK ADVQGSVEAL AASLLKIDVE GVRVNVVHSA
     VGAINESDIT LAEASDAVVI GFNVRPTPQA RQQAETDEVE IRLHSIIYKV IEEIEDAMKG
     MLDPEFEEKI IGEAVIRETF KVSKVGTIGG FMVTNGKITR DSSARVIRDG VVIFDGKLAS
     LKHYKDDVKE VGNAQEGGLT IENYNDIKVD DVIEAYIMEE IKR