IF2_YERPG
ID IF2_YERPG Reviewed; 884 AA.
AC A9R5A3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=YpAngola_A3993;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX84875.1; -; Genomic_DNA.
DR RefSeq; WP_012230159.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R5A3; -.
DR SMR; A9R5A3; -.
DR KEGG; ypg:YpAngola_A3993; -.
DR PATRIC; fig|349746.12.peg.717; -.
DR OMA; NRDNRTG; -.
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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..884
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093848"
FT DOMAIN 383..552
FT /note="tr-type G"
FT REGION 93..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 528..530
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 102..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 884 AA; 96608 MW; 1AAB10345BE069A8 CRC64;
MTDVTVKSLA AEIQTPVDRL VQQFADAGIK KSDVDSVTQQ EKEILLAHLN REHGSVPNKL
TLQRKTRSTL NIPSTGGKSK SVQIEVRKKR TYVNTPEAEQ AKAEEQAQRE AEATAQKIAE
EKAKREAEEQ AKREAAEKAK RQAAEKEKVT NQQTDEKTKP AQTDKARREA EAAELKRSVE
EETRRKVEED AKRVAEEARK MAAENEGKWP EPVAEQTESA DYHVTTSQHA RAAEDENDAK
VEGDRRSRTR GGKATKQKKG NKLSESKADR EEARAVGRKG KRKPSTLQQS FNKPVVAVNR
DVVIGETVTV AELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA EEIGHKVILR
RENELEEALM SDRDIGVEAA AEHRAPVVTI MGHVDHGKTS LLDYIRSTKV ASGEAGGITQ
HIGAYHVETE NGMITFLDTP GHAAFTSMRA RGAQATDIVV LVVAADDGVM PQTIEAIQHA
KAANVPVVVA VNKIDKPEAD PDRVKTELSQ YGIQPEEWGG ESQFINVSAK AGIGIDELLN
AILLQAEVLE LKAVRTGMAN GVVIESFLDK GRGPVATVLV QQGTLNKGDI VLCGFEYGRV
RAMRDELGRD ITSAGPSIPV EILGLSSVPA AGDEVTVVRD EKKAREVALY RQGKFREVKL
ARQQKSKLEN MFANMTEGEV SELNIVIKSD VQGSCEAICD SLEKLSTDEV KVRIVGSGVG
GITETDATLA AASGAIILGF NVRADASARR VVETEGLDLR YYSVIYSLID EVKQAMSGML
APEYKQQIIG LAEVRDVFKS PKFGAIAGCM VTEGVIKRNN PIRVLRDNVV IYEGELESLR
RFKDDVSEVR NGMECGIGVK NYNDVRTGDV IEVFEIIEIK RTIA
