IF2_LEPBL
ID IF2_LEPBL Reviewed; 864 AA.
AC Q04ZJ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LBL_2087;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
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; CP000348; ABJ79500.1; -; Genomic_DNA.
DR RefSeq; WP_011670553.1; NC_008508.1.
DR AlphaFoldDB; Q04ZJ5; -.
DR SMR; Q04ZJ5; -.
DR KEGG; lbl:LBL_2087; -.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 55867at2; -.
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..864
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335486"
FT DOMAIN 359..528
FT /note="tr-type G"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..375
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 393..397
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 414..417
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 468..471
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 504..506
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 184..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368..375
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 414..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 468..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 864 AA; 92440 MW; 064A789572A5F98C CRC64;
MEDKNKTIKE TLQGAADAGK RKKLIIKKKG DENSAPSSAS PKKETIAESA PVKPLTPLPS
RGDSGQSPIV RPAPSASKEV KYEESSRKQD SGQSGSRPLR DKDSQVRPSG DSSYPVSRSP
FQKEDSNIIV SRPTQRPVRP NPGGSYQGNR GPGQGGGYQG NRGPGQGGGY QGNRGPGQGG
GYQGNRGPGQ QTGPGNRFGG SGPGNRSGGP GGRPMPITSA EVELSQARGS TGASKKKGHD
KEKTSSDKRD FSGAENTKFF KQRFKKTKVV GVSGVSVPKE ITVLENVQVG ELAKKMNLKP
GDVIGKLMKM GMMVTINNII DAETAALLAD EYGCKVKVVS LYEETIIEEE KDNEGDYINR
PPVVTIMGHV DHGKTKLLDT IRRSSVIDTE SGGITQHIGA YQVKTARGLI TFLDTPGHEA
FTSMRARGAK VTDIVILVVA ADDGVMPQTL EAISHAKAAE VPIIVAINKI DLPTANPDKI
MQELANHGLQ SEEWGGQTMY VKISARENIG IDKLLEVILL QAEVMDLKAN PKRRAKGTII
EAKLDPGRGS VATVLIQNGT LRVGDPFVAG VFSGRVRAMY NDLGQLIEEA GPAFPAQVTG
IDGVPDAGAP FDAMADEKEA RNISQHRIEF EKIGNAGAAA GTTSKVTLEN MNEYIKLGAL
KELKVIIKAD VRGSAEAIKE SLEKLSTPEV KLNVIQSGAG AIVDMDVMLA SASNALIIGF
HVRANPKTIA LAEKEQVQIK YYNIIYQVVD EIKLAMEGLL EPEKIEEVIG TAEIREIFKV
SKIGNIAGCM VTSGKIQKSA NVRVISDGVT KFDGKLKSLK RVKDDVNDVV SGFECGIQVD
GYNDFKVGDT IEAYNVTVIK RKLE
