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 27-MAR-2024, entry version 118.
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; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC 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 PaxDb; 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 OrthoDB; 9811804at2; -.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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
//
