ID   IF2_STRTD               Reviewed;         943 AA.
AC   Q03M88;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=STER_0383;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000419; ABJ65684.1; -; Genomic_DNA.
DR   RefSeq; WP_011680757.1; NC_008532.1.
DR   AlphaFoldDB; Q03M88; -.
DR   SMR; Q03M88; -.
DR   KEGG; ste:STER_0383; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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..943
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008357"
FT   DOMAIN          445..614
FT                   /note="tr-type G"
FT   REGION          29..349
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        29..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;  103824 MW;  E66470CAF95BBC1B CRC64;
     MSKKRLYEIA KEVGVESKVI VAKAQELGLS VKSHSSSVEE ADANRITSSL KAGTAKDESK
     PAPKATPTPK EEKVEPKVDK ASVAKSAPAK ETSKAEVKEA SVALKKPKSR NFKAEREARA
     KAEAERRKNG GGRDNRNRNQ QGNDQGKRHN NDRRNQKGNG QGDHNKGNRD NSTNHDRNFQ
     GKLRNDQNQN NRRDNARNNQ AGPRIDLKAR AAALKAEQNA EYSRQSETRF REEKAAEQRR
     AKEQEKARKE KQQAEVAVQK AAAETKPAPK PAPVAPQSAP TAQVQDTRRK KVRPNKSRDN
     HRVNEDGPKQ TRNNKWNNQN QVRNQRNSNW NKNKNKKGKN NRGNSAPKLV 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
//