IF2_UREU1
ID IF2_UREU1 Reviewed; 614 AA.
AC B5ZBC9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=UUR10_0326;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001184; ACI60166.1; -; Genomic_DNA.
DR RefSeq; WP_012560304.1; NC_011374.1.
DR AlphaFoldDB; B5ZBC9; -.
DR SMR; B5ZBC9; -.
DR STRING; 565575.UUR10_0326; -.
DR EnsemblBacteria; ACI60166; ACI60166; UUR10_0326.
DR GeneID; 45015873; -.
DR KEGG; uue:UUR10_0326; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_14; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002018; 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; 1.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..614
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093842"
FT DOMAIN 115..283
FT /note="tr-type G"
FT REGION 124..131
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 149..153
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 170..173
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 224..227
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 260..262
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 124..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 170..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 224..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 614 AA; 67760 MW; FDE14FE88A7AB9D2 CRC64;
MAKKNIKQKK DNRIAIDVKK HIKKVDVGVF GGTFVFTSPL SIAELAPKLN KSTNEIIMRY
FKKGVVYNLN TILDEEQIGE LCLEYDLDFK IEKNVNTENL LENIAFDDLE ADLVARAPIV
TIMGHVDHGK TTLLDTIRKS SVTASEAGGI TQHIGAYQIL KGDKPITFID TPGHEAFTEM
RARGANLTDI VILVVAADDG IKMQTEEAID HAKAANVPII VFVNKMDKYE ANPDKVLNQL
SAKEIVAEEL GGDIVFVKGS ALKNEGIFEL LDSILLIAEL NDYKANPNRL AYGTTIEANL
DKGHGPLATL LVQNGTLRKG DYLVVGSTYG KIRNMFDEYD NEIEMALPSK PVKVSGFEEV
PTAGDKFLAL ADEKQARAIA NDVKQKKIRL ERSMLQSSDI RAKIANGELK NINLIIKADV
QGSLEALKGI FNSINIEGVT TTLVRSAIGT ISESDVRLAQ TSDAIIIGFN VRANRIIKDL
ADSVGVQIMN YDIIYKFKED LEAWMKGTLD PIIVEEVIGE AKVLKLFKHS QVGTICGCRV
INGKIKRNAL VRVLRDGIVI YNSKIATLQH NKDSVNEVIA DKECGLTIAN FNDVKENDII
EVYVKVEKNH DEVK