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IF2_LACDB
ID   IF2_LACDB               Reviewed;         825 AA.
AC   Q049V5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LBUL_1241;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
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; CP000412; ABJ58767.1; -; Genomic_DNA.
DR   RefSeq; WP_003618592.1; NC_008529.1.
DR   AlphaFoldDB; Q049V5; -.
DR   SMR; Q049V5; -.
DR   KEGG; lbu:LBUL_1241; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   BioCyc; LDEL321956:LBUL_RS05825-MON; -.
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; 1.
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..825
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008261"
FT   DOMAIN          326..495
FT                   /note="tr-type G"
FT   REGION          1..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..342
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          360..364
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          381..384
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          435..438
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          471..473
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335..342
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         381..385
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         435..438
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   825 AA;  90849 MW;  0EA0A93A7D26A7A0 CRC64;
     MTKKQENETS KELGMDNKKT SGKSGKLKIS VSAIRKGEKK TEGKRSNARR RANNHSNDHS
     KRRRPAAQDL LKDLKQKQRA DEARLDQESK AAKQEYKKSL NKAEASESKP VVKKVESVEK
     PAETAAEAPK VRGPKILKPS PARLKQNQAN SEKPAAKPSS SRRPSSRPSF TEAPMPENKE
     GRRRKSGKPG RKGQNSYADQ GRGANSNRSE QRKRKNKKHQ SAPQVKKQVT QRKDRPLPES
     FEYEVGMNAQ DLGKILHREP AEIVKKLFML GIMINQNRSL DKDTIELLAA DYGIEAVEKV
     HEDISDIDNI FAQEMEESKN SENQVVRPPV VTIMGHVDHG KTTLLDRLRH TRVSEHEAGG
     ITQNIGAYQV RINDRLITFL DTPGHAAFSS MRARGAEITD IVVLIVAADD GVMPQTIEAI
     DHAKSAGVPI IVAINKMDRP GANPAHVTEQ LMQYELIPEN YGGSTIFVNI SAKTGMGIDE
     LLENIILEAD MLELKADPKQ KAIGTVVEAR LSRGKGPVAD VLIQQGTLRV GDPIVVGDTF
     GRVRTMTNDK GHQVKKATPS MPVEITGLND VPESADKLVV FADEKTARAV GEARAQQSLQ
     KQRENVQHVT LDNLFDTMKR ESMKSVDIVL KADVQGSAEA LAQSFQKIDV EGVRVNIIHS
     GVGAINESDV TLASASNALI IGFNVRPTAT AKSQAAQEGV DIRLYSIIYK AIDDVKAAMQ
     GMLEPTYEEK VIGNLTVRET WKVSKIGTIA GAFVDNGYVT RESGIRVIRD GVVKYDGKVA
     SLRRFKDDVK EVKAGFDCGL TIENFNDIKE GDELEAYEMQ EVKPG
 
 
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