IF2_LYSSC
ID IF2_LYSSC Reviewed; 758 AA.
AC B1HR05;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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=Bsph_1598;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA39196.1; -; Genomic_DNA.
DR RefSeq; WP_012293304.1; NC_010382.1.
DR AlphaFoldDB; B1HR05; -.
DR SMR; B1HR05; -.
DR EnsemblBacteria; ACA39196; ACA39196; Bsph_1598.
DR KEGG; lsp:Bsph_1598; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002164; 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.
FT CHAIN 1..758
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093801"
FT DOMAIN 259..428
FT /note="tr-type G"
FT REGION 55..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..275
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 293..297
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 314..317
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 368..371
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 404..406
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268..275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 314..318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 368..371
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 758 AA; 83264 MW; 91E4CC40EF3546E0 CRC64;
MTKIRVHEYA KQVNKTSKEV IEALSKLNVS VTNHMSMLEK DIVSKLNQTF KATPEKNVGK
QATQNISQKS QSNGQQNHSV KKQEGQRQQS ATSKPKVNNQ QHSNSSNEKS KNTKGNQNRN
MTQNNNNNNN NNNNNRRGGG GYNQRPKPGI HGGKRRHPKT HQPSIPVKQK ELPEKITFVE
SLSVAELAKK LHREPSEIIK KLFMLGVMAT INQELDKDAI ELICADYGVE VEEEIRVDIT
DLETHFEQTE EVNEAQLSER PPVVTIMGHV DHGKTTLLDS IRNTKVTAGE AGGITQHIGA
YQVTEGDKKI TFLDTPGHAA FTTMRARGAK VTDLTILVVA ADDGVMPQTV EAINHAKAAE
VPIIVAVNKM DKPSANPDRV MQELTEHGLV PEAWGGETIF VPISALKGEG IDTLLEMILL
VAEVGELKAN PDRLALGTVI EAQLDKGRGS VATLLVQDGT LKVGDPIVVG HTFGRVRAMV
NDKGRRVKEA GPSTPVEITG LNDVPQAGDR FVVFEDEKTA RQVGETRAMS AIQAQRSEKQ
RVTLDNLFEQ MSQGEMKELN LIVKADVQGT VEAMAASLMK IDVEGVNVKI IHTGAGAITE
SDISLAAASN AIVIGFNVRP DVNAKRAAEE EGVDIRLHRI IYKVIEEIEQ AMKGMLDPEF
EEKIIGQAEV RQTIKVSKVG TIAGSYVTEG KVTRDSGVRV IRDNVVIFEG ELDTLKRFKD
EVKEVARGYE CGITITNFND IKEGDIIEAY IMEEVKRV
