IF2_MYCUA
ID IF2_MYCUA Reviewed; 945 AA.
AC A0PQC4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MUL_2122;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL04543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PQC4; -.
DR SMR; A0PQC4; -.
DR STRING; 362242.MUL_2122; -.
DR EnsemblBacteria; ABL04543; ABL04543; MUL_2122.
DR KEGG; mul:MUL_2122; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000000765; 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.
FT CHAIN 1..945
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008285"
FT DOMAIN 441..612
FT /note="tr-type G"
FT REGION 47..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..457
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 475..479
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 590..592
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 105..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 450..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 554..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 945 AA; 97995 MW; 40A7530CEC0BD849 CRC64;
MAGKARVHEL AKELGVTSKE VLARLSEQGE FVKSASSTVE APVARRLRES FGGGKSAPAK
GSDTGAAKGV AKAPQKVSGA SPAAKAPDRS LDAALDKAVG NGAPAPVPAP APAPTPAPAP
AQPADSGVAP PAATPAAPAA SAAPAPPKAP LPGQRPAPTP GKPAAPQAPH PGMAPGARPG
PVPKQGVRTP RVGNNPFSSA QPVDRPIPRP QAPRPGAPRP GAPRPGGASS GNMPPRPGGA
SGGPRPPRTG APRPGGGRPG GPGGGRSDGG GGNYRGGGGG VGAAPGGGFR GRPGGGGGGG
RPGQRGGAAG AFGRPGGAPR RGRKSKRAKR AEYENMQAPV VGGVRLPHGN GETIRLARGA
SLSDFADKIN ANPAALVQAL FNLGEMVTAT QSVGDETLEL LGSEMNYNVQ VVSPEDEDRE
LLESFDLTYG EDSGDESELQ TRPPVVTVMG HVDHGKTRLL DTIRKANVRE GEAGGITQHI
GAYQVSVDHD GTERLITFID TPGHEAFTAM RARGAKATDI AILVVAADDG VMPQTVEAIN
HAQAADVPIV VAVNKIDKEG ADPAKIRGQL TEYGLVAEDF GGDTMFVDIS AKQGTNIEAL
EEAVLLTADA ALDLRANPDM EAQGVAIEAH LDRGRGPVAT VLVQRGTLRV GDSVVAGDAY
GRVRRMVDEH GEDVEEALPS RPVQVIGFTS VPGAGDNFLV VDEDRIARQI ADRRSARKRN
ALAARSRKRI SLEDLDSALK ETSQLNLILK GDNAGTVEAL EEALMGIEVD DEVALRVIDR
GVGGITETNV NLASASDAII IGFNVRAEGK ATELANREGV EIRYYSVIYQ AIDEIEKALR
GMLKPIYEEV ELGRAEIRAL FRSSKVGLIA GCMISSGVVR RNAKARLLRD NIVVVENLSI
RSLRREKDDV TEVREGFECG MTLGYSDLKE GDFIESYELV QKDRS
