IF2_BACLD
ID IF2_BACLD Reviewed; 716 AA.
AC Q65JI1; Q62UY6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=BLi01888, BL01224;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(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; AE017333; AAU40783.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23423.1; -; Genomic_DNA.
DR RefSeq; WP_009328498.1; NC_006322.1.
DR AlphaFoldDB; Q65JI1; -.
DR SMR; Q65JI1; -.
DR STRING; 279010.BL01224; -.
DR PRIDE; Q65JI1; -.
DR EnsemblBacteria; AAU23423; AAU23423; BL01224.
DR GeneID; 66216101; -.
DR KEGG; bld:BLi01888; -.
DR KEGG; bli:BL01224; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; BLIC279010:BLI_RS09340-MON; -.
DR Proteomes; UP000000606; 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; Reference proteome.
FT CHAIN 1..716
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228166"
FT DOMAIN 217..386
FT /note="tr-type G"
FT REGION 50..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..233
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 251..255
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 272..275
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 326..329
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 362..364
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 272..276
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 326..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 716 AA; 78578 MW; FCD51846897955C9 CRC64;
MAKMRVYEYA KAINVSSKDI IAALKDMNIE VNNHMAMIEE NAIKQLDQKF KKSAKPAGNK
KDAGTGGQKP QQEAAKLNAG SKPNKNRDGK KNNVQNTQFN NKNKKKNNNN KKNKRGKNHQ
SPQEKQFKPK KELPEKIEFT NSMSVGALAE ELGKEPSEII KKLMLLGIMA TINQDLDKDT
VELIASEYGV EVEEVIVHEE TEFEKYEEPD NEEDLEIRPP VVTIMGHVDH GKTTLLDSIR
KTKVVEGEAG GITQHIGAYQ IEENGKKITF LDTPGHAAFT TMRARGAEVT DITILVVAAD
DGVMPQTVEA INHAKAAEVP IIVAVNKIDK PTANPDRVMQ ELTEHGLVPE AWGGETIFVP
LSALSGEGID ELIEMILLVS EVEELKANPN RRAKGTVIEA ELDKGKGSVA TLLVQNGTLH
VGDPIVVGNT FGRVRAMVND VGRRVKSAGP STPVEITGLN EVPNAGDQFL VFKDEKTARS
VGEARATKQL EEQRSDKAKL SLDDLFEQIK QGDVKEINLV VKADVQGSVE ALAAALQKIE
VEGVRVKIIH TGVGAITESD IILASASNAI VIGFNVRPDG NAKSTAEAEN VDIRLHRIIY
KVIDEIEAAM KGMLDPEYEE KVIGMVEVRQ TFKVSKIGTI AGGYVTEGTI TRDSGIRLIR
DGVVIFEGEV DVLKRFKDDV KEVSQGYECG ITIKKYNDIR EGDMIEAYVM QEIERK
