IF2_LEPBJ
ID IF2_LEPBJ Reviewed; 852 AA.
AC Q04U31;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LBJ_0946;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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; CP000350; ABJ75589.1; -; Genomic_DNA.
DR RefSeq; WP_011671660.1; NC_008510.1.
DR AlphaFoldDB; Q04U31; -.
DR SMR; Q04U31; -.
DR EnsemblBacteria; ABJ75589; ABJ75589; LBJ_0946.
DR KEGG; lbj:LBJ_0946; -.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000656; Chromosome 1.
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..852
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335485"
FT DOMAIN 347..516
FT /note="tr-type G"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..363
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 381..385
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 402..405
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 456..459
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 492..494
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 456..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 852 AA; 91283 MW; 60F71D1EF90730EA CRC64;
MEDKNKTIKE TLQGAADAGK RKKLIIKKKG DENSAPSSAS PKKETIAESA PVKPLTPLPS
RGDSGQSPIV RPAPSASKEV KYEESSRKQD SGQSGSRPLR DKDSQVRPSG DSSYPVSRSP
FQKEDSNIIV SRPTQRPVRP NPGGSYQGNR GPGQGGGYQG NRGPGQGGGY QGNRGPGQQT
GPGNRFGGSG PGNRSGGPGG RPMPITSAEV ELSQARGSTG ASKKKGHDKE KTSSDKRDFS
GAENTKFFKQ RFKKTKVVGV SGVSVPKEIT VLENVQVGEL AKKMNLKPGD VIGKLMKMGM
MVTINNIIDA ETAALLADEY GCKVKVVSLY EETIIEEEKD NEGDYINRPP VVTIMGHVDH
GKTKLLDTIR RSSVIDTESG GITQHIGAYQ VKTARGLITF LDTPGHEAFT SMRARGAKVT
DIVILVVAAD DGVMPQTLEA ISHAKAAEVP IIVAINKIDL PTANPDKIMQ ELANHGLQSE
EWGGQTMYVK ISARENIGID KLLEVILLQA EVMDLKANPK RKAKGTIIEA KLDPGRGSVA
TVLIQNGTLR VGDPFVAGVF SGRVRAMYND LGQLIEEAGP AFPAQVTGID GVPDAGAPFD
AMADEKEARN ISQHRIEFEK IGNAGAAAGT TSKVTLENMN EYIKLGALKE LKVIIKADVR
GSAEAIKESL EKLSTPEVKL NVIQSGAGAI VDMDVMLASA SNALIIGFHV RANPKTIALA
EKEQVQIKYY NIIYQVVDEI KLAMEGLLEP EKIEEVIGTA EIREIFKVSK IGNIAGCMVT
SGKIQKSANV RVISDGVTKF DGKLKSLKRV KDDVNDVVSG FECGIQVDGY NDFKVGDTIE
AYNVTVIKRK LE
