ID   IF2_LEPIN               Reviewed;         863 AA.
AC   Q8F7K1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LA_0943;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
RN   [2]
RP   SEQUENCE REVISION TO 51 AND 65.
RA   Zhong Y., Zheng H.-J., Wang S.-Y., Guo X.-K., Zhao G.-P.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; AE010300; AAN48142.2; -; Genomic_DNA.
DR   RefSeq; NP_711124.2; NC_004342.2.
DR   RefSeq; WP_000389638.1; NC_004342.2.
DR   AlphaFoldDB; Q8F7K1; -.
DR   SMR; Q8F7K1; -.
DR   STRING; 189518.LA_0943; -.
DR   EnsemblBacteria; AAN48142; AAN48142; LA_0943.
DR   KEGG; lil:LA_0943; -.
DR   PATRIC; fig|189518.3.peg.945; -.
DR   HOGENOM; CLU_006301_5_1_12; -.
DR   InParanoid; Q8F7K1; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..863
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137216"
FT   DOMAIN          358..527
FT                   /note="tr-type G"
FT   REGION          1..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..374
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          392..396
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          413..416
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          467..470
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          503..505
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        80..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         367..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         413..417
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         467..470
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   863 AA;  91962 MW;  8349570B086E695C CRC64;
     MEDKNKTIKE TLQGSADAGK RKKLIIKKKG DDPSTPSPAA SPKKETVAES APSSKPPVMP
     LPLPGDSGQS PIVRPAPSSH SPAKREESPG KQDAGRPPRD KDTRQGGGSS YPPSRSPFQK
     EDSNIIVSRP IQRTGPSRPN SGGGYQGNRG PGQGGGGYQG NRGPGQGGGG YQGNRGPGPG
     QGGGGYQGNR GPGQGGGGYQ GNRGPRSGGT GTRPMPITSA EVELSQSRGS SVTSKKKGHD
     KEKSTSDRDF SGAENTKFFK QKFKKTKVVG VSGVSVPKEI TLLENVQVGE LAKKMNLKPG
     DVIGKLMKMG MMVTINNIID AETAALLADE YGCKVKVVSL YEETIIEEEK DNQEDYINRP
     PVVTIMGHVD HGKTKLLDTI RRSSVIDTES GGITQHIGAY QVRTARGLIT FLDTPGHEAF
     TSMRARGAKV TDIVVLVVAA DDGVMPQTLE AISHAKAAEV PILVAINKID LPAANPEKIM
     QELANHGLQS EEWGGETMYA KISARENIGI DKLLEMILLQ AEVMDLKANP KRRAKGTIIE
     AKLDPGRGSV ATVLIQNGTL RVGDPFVAGV FSGRVRAMYN DLGQLIQEAG PAFPAQVTGI
     DGVPDAGAPF DAMADEKEAR NISQHRIEFE RIGNAGAATG TSSKVTLENM NEFIKQGALK
     ELKVIIKADV RGSAEAIKES LEKLSTPEVK LNVIQSGAGA IVDMDVMLAS ASNALIIGFH
     VRANPKTIAL AEKEGVQIKY YNIIYQVVDE IKLAMEGLLE PEKIEEVIGT AEIREIFKVS
     KIGNIAGCMV LSGKIQKSAN IRVIGDGVTK FEGKLKSLKR VKDDVNDVVA GFECGIQVDG
     YNDFKVGDTI EAYNVTVIKR KLE