ID   IF2_UREPA               Reviewed;         614 AA.
AC   Q9PQH1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=UU320;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30729.1; -; Genomic_DNA.
DR   RefSeq; WP_006688753.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQH1; -.
DR   SMR; Q9PQH1; -.
DR   STRING; 273119.UU320; -.
DR   EnsemblBacteria; AAF30729; AAF30729; UU320.
DR   GeneID; 29672437; -.
DR   KEGG; uur:UU320; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000423; 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; Reference proteome.
FT   CHAIN           1..614
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137278"
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;  68049 MW;  A41FF74375609876 CRC64;
     MAKKNIKQKK DNRIAIDVKK HIKKVDVGVF DGTFVFTSPL SISELAPKLN KSPNEIIMRY
     FKKGVVYNLN TILDEEQIGE LCLEYDLDFK IEKNVNTENL LENIYFDDLE IDLVARAPIV
     TIMGHVDHGK TTLLDTIRKS SITASEAGGI TQHIGAYQII KDNRAITFID TPGHEAFTEM
     RARGANLTDI VILVVAADDG IKMQTEEAID HAKAANVPII VFVNKMDKYE ANPEKVLNQL
     SAKEIVAEEL GGDVVFVKGS ALKNEGISEL LDSILLIAEL NNYKANPNRL AYGTTIEANL
     DKGHGPLATL LVQNGTLRKG DYLVVGSTYG KIRNMFDEYD NEIEIALPSK PVKVSGFEEV
     PTAGDKFLAL ADEKQARAIA NDVKQKKMRL ERAMLQSSDI RTKIANGELK NINLIIKADV
     QGSLEALKGI FSSINIEGVT TTLIRSAIGT ISESDVRLAQ TSDAIIIGFN VRASRIIKDL
     ADSVGVQIMN YDIIYKFKED LELWMKGTLD PIIIEEVIGE AKVLKLFKHS QVGTICGCRV
     INGKIKRNAL VRVLRDGIVI YNSKIATLQH NKDSVNEVIA DKECGLTIAN FNDIKENDII
     EVYIKVEKKH DEVK