IF2_LACDA
ID IF2_LACDA Reviewed; 825 AA.
AC Q1G9P9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ldb1332;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI98133.1; -; Genomic_DNA.
DR RefSeq; WP_011544002.1; NZ_JQAV01000006.1.
DR AlphaFoldDB; Q1G9P9; -.
DR SMR; Q1G9P9; -.
DR STRING; 390333.Ldb1332; -.
DR EnsemblBacteria; CAI98133; CAI98133; Ldb1332.
DR KEGG; ldb:Ldb1332; -.
DR PATRIC; fig|390333.13.peg.1699; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR BioCyc; LDEL390333:LDB_RS05695-MON; -.
DR Proteomes; UP000001259; 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; 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; Reference proteome.
FT CHAIN 1..825
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008260"
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; 90866 MW; 71745DC824665A13 CRC64;
MTKKQENETS KELGMDNKKT SGKSGKLKIS VSAIRKGEKK TEGKRSNTRR RANNHSNDHS
KRRRPAAQDL LKDLKQKQRA DEARLDQESK AAKQEYKKSL NKAEASESKP VVKKVESVEK
PAETAAEAPK VRGPKILKPS PARLKQNQAN SEKPAAKPSS SRRPSSRPSF TEAPMPENKE
GRRRKSGKPG RKGQNSYADQ GRGANSNRSE QRKRKNKKHQ SAPQVKKQVT QRKDRPLPES
FEYEVGMNAQ DLGKILHREP AEIVKKLFML GIMINQNLSL 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 EVKPS
