IF2_LEPIC
ID IF2_LEPIC Reviewed; 874 AA.
AC Q72NX3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LIC_12705;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS71263.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE016823; AAS71263.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000389641.1; NC_005823.1.
DR AlphaFoldDB; Q72NX3; -.
DR SMR; Q72NX3; -.
DR PaxDb; Q72NX3; -.
DR EnsemblBacteria; AAS71263; AAS71263; LIC_12705.
DR GeneID; 61142585; -.
DR KEGG; lic:LIC_12705; -.
DR HOGENOM; CLU_006301_5_1_12; -.
DR Proteomes; UP000007037; Chromosome I.
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..874
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137215"
FT DOMAIN 369..538
FT /note="tr-type G"
FT REGION 1..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..385
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 403..407
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 424..427
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 478..481
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 514..516
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 244..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..385
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 424..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 874 AA; 92994 MW; 001F8809E2DBECB0 CRC64;
MEDKNKTIKE TLQGSADAGK RKKLIIKKKG DDPSTPSPAA SPKKETVAES APSSKPPVMP
LPLPGDSGQS PIVRPAPSSH SPAKREESPG KQDAGRPPRD KDTRQGGGSS YPPSRSPFQK
EDSNIIVSRP IQRTGPSRPN SGGGYQGNRG PGQGGGGYQG NRGPGQGGGG YQGNRGPGQG
GGGYQGNRGP GQGGGGYQGN RGPGQGGGGY QGNRGPRSGG TGTRPMPITS AEVELSQSRG
SSVTSKKKGH DKEKSTSDRD FSGAENTKFF KQKFKKTKVV GVSGVSVPKE ITLLENVQVG
ELAKKMNLKP GDVIGKLMKM GMMVTINNII DAETAALLAD EYGCKVKVVS LYEETIIEEE
KDNQEDYINR PPVVTIMGHV DHGKTKLLDT IRRSSVIDTE SGGITQHIGA YQVRTARGLI
TFLDTPGHEA FTSMRARGAK VTDIVVLVVA ADDGVMPQTL EAISHAKAAE VPILVAINKI
DLPAANPEKI MQELANHGLQ SEEWGGETMY AKISARENIG IDKLLEMILL QAEVMDLKAN
PKRRAKGTII EAKLDPGRGS VATVLIQNGT LRVGDPFVAG VFSGRVRAMY NDLGQLIQEA
GPAFPAQVTG IDGVPDAGAP FDAMADEKEA RNISQHRIEF ERIGNAGAAT GTSSKVTLEN
MNEFIKQGAL KELKVIIKAD VRGSAEAIKE SLEKLSTPEV KLNVIQSGAG AIVDMDVMLA
SASNALIIGF HVRANPKTIA LAEKEGVQIK YYNIIYQVVD EIKLAMEGLL EPEKIEEVIG
TAEIREIFKV SKIGNIAGCM VLSGKIQKSA NIRVIGDGVT KFEGKLKSLK RVKDDVNDVV
AGFECGIQVD GYNDFKVGDT IEAYNVTVIK RKLE
