IF2_GEOKA
ID IF2_GEOKA Reviewed; 709 AA.
AC Q5L0I8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GK1263;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD75548.1; -; Genomic_DNA.
DR RefSeq; WP_011230763.1; NC_006510.1.
DR AlphaFoldDB; Q5L0I8; -.
DR BMRB; Q5L0I8; -.
DR SMR; Q5L0I8; -.
DR STRING; 235909.GK1263; -.
DR EnsemblBacteria; BAD75548; BAD75548; GK1263.
DR KEGG; gka:GK1263; -.
DR PATRIC; fig|235909.7.peg.1363; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; LYAWPWP; -.
DR Proteomes; UP000001172; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..709
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228199"
FT DOMAIN 240..409
FT /note="tr-type G"
FT REGION 47..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..256
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 274..278
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 295..298
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 349..352
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 385..387
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 47..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 295..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 349..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 709 AA; 78241 MW; 0CD7FA3B936639EC CRC64;
MSKMRVYEYA KKQNVPSKDV IHKLKEMNIE VNNHMAMLEA DVVEKLDHQY RPNTGKKEEK
KAEKKTEKPK RPTPAKAADF ADEEIFDDSK EAAKMKPAKK KGAPKGKETK KTEAQQQEKK
LLQAAKKKGK GPAKGKKQAA PAAKQAPQPA KKEKELPKKI TFEGSLTVAE LAKKLGREPS
EIIKKLFMLG VMATINQDLD KDAIELICSD YGVEVEEKVT IDETNFEAIE IVDAPEDLVE
RPPVVTIMGH VDHGKTTLLD AIRHSKVTEQ EAGGITQHIG AYQVTVNDKK ITFLDTPGHE
AFTTMRARGA QVTDIVILVV AADDGVMPQT VEAINHAKAA NVPIIVAINK IDKPEANPDR
VMQELMEYNL VPEEWGGDTI FCKLSAKTKE GLDHLLEMIL LVSEMEELKA NPNRRAVGTV
IEAKLDKGRG PVATLLIQAG TLRVGDPIVV GTTYGRVRAM VNDSGRRVKE ATPSMPVEIT
GLHEVPQAGD RFMVFEDEKK ARQIAEARAQ RQLQEQRSVK TRVSLDDLFE QIKQGEMKEL
NLIVKADVQG SVEALVAALQ KIDVEGVRVK IIHAAVGAIT ESDISLATAS NAIVIGFNVR
PDANAKRAAE SEKVDIRLHR IIYNVIEEIE AAMKGMLDPE YEEKVIGQAE VRQTFKVSKV
GTIAGCYVTD GKITRDSKVR LIRQGIVVYE GEIDSLKRYK AIAPNGARV
