IF2_MYCLE
ID IF2_MYCLE Reviewed; 924 AA.
AC Q9Z5I9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=ML1556; ORFNames=MLCB596.14;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL035472; CAB36570.1; -; Genomic_DNA.
DR EMBL; AL583922; CAC30507.1; -; Genomic_DNA.
DR PIR; F87103; F87103.
DR RefSeq; NP_302081.1; NC_002677.1.
DR RefSeq; WP_010908402.1; NC_002677.1.
DR AlphaFoldDB; Q9Z5I9; -.
DR SMR; Q9Z5I9; -.
DR STRING; 272631.ML1556; -.
DR EnsemblBacteria; CAC30507; CAC30507; CAC30507.
DR KEGG; mle:ML1556; -.
DR PATRIC; fig|272631.5.peg.2936; -.
DR Leproma; ML1556; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000000806; Chromosome.
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; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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..924
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137223"
FT DOMAIN 420..591
FT /note="tr-type G"
FT REGION 118..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..436
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 454..458
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 479..482
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 533..536
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 569..571
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 144..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429..436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 479..483
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 533..536
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 924 AA; 96651 MW; 34605A1069001224 CRC64;
MAGKARVHEL AKELGVTSKE VLARLNEQGE FVKSASSTVE APVARRLRES FGGIKPAADK
GAEQVATKAQ AKRLGESLDQ TLDRALDKAV AGNGATTAAP VQVDHSAAVV PIVAGEGPST
AHREELAPPA GQPSEQPGVP LPGQQGTPAA PHPGHPGMPT GPHPGPAPKP GGRPPRVGNN
PFSSAQSVAR PIPRPPAPRP SASPSSMSPR PGGAVGGGGP RPPRTGVPRP GGGRPGAPVG
GRSDAGGGNY RGGGVGALPG GGSGGFRGRP GGGGHGGGGR PGQRGGAAGA FGRPGGAPRR
GRKSKRQKRQ EYDSMQAPVV GGVRLPHGNG ETIRLARGAS LSDFAEKIDA NPAALVQALF
NLGEMVTATQ SVGDETLELL GSEMNYNVQV VSPEDEDREL LEPFDLTYGE DQGDEDELQV
RPPVVTVMGH VDHGKTRLLD TIRKANVREA EAGGITQHIG AYQVGVDLDG SERLITFIDT
PGHEAFTAMR ARGAKATDIA ILVVAADDGV MPQTVEAINH AQAADVPIVV AVNKIDKEGA
DPAKIRGQLT EYGLVAEDFG GDTMFIDISA KVGTNIEALL EAVLLTADAA LDLRANSGME
AQGVAIEAHL DRGRGPVATV LVQRGTLRIG DSVVAGDAYG RVRRMVDEHG VDIEAALPSS
PVQVIGFTSV PGAGDNFLVV DEDRIARQIA DRRSARKRNA LAARSRKRIS LEDLDSALKE
TSQLNLILKG DNAGTVEALE EALMGIQVDD EVALRVIDRG VGGITETNVN LASASDAIII
GFNVRAEGKA TELASREGVE IRYYLVIYQA IDDIEKALRG MLKPIYEENQ LGRAEIRALF
RSSKVGIIAG CIISSGVVRR NAKVRLLRDN IVVTDNLTVT SLRREKDDVT EVREGFECGM
TLGYSDIKEG DVIESYELVE KQRA
