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IF2_THIDA
ID   IF2_THIDA               Reviewed;         922 AA.
AC   Q3SKX1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tbd_0697;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96650.1; -; Genomic_DNA.
DR   RefSeq; WP_011311209.1; NC_007404.1.
DR   AlphaFoldDB; Q3SKX1; -.
DR   SMR; Q3SKX1; -.
DR   STRING; 292415.Tbd_0697; -.
DR   EnsemblBacteria; AAZ96650; AAZ96650; Tbd_0697.
DR   KEGG; tbd:Tbd_0697; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000008291; 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; IPR009061; DNA-bd_dom_put_sf.
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; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
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; Reference proteome.
FT   CHAIN           1..922
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228256"
FT   DOMAIN          422..589
FT                   /note="tr-type G"
FT   REGION          243..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..438
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          456..460
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          477..480
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          531..534
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          567..569
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        267..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         431..438
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         477..481
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         531..534
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   922 AA;  97801 MW;  B79B3B058483EE90 CRC64;
     MNVEQFAQEL KLPPQLLLEQ LKAAGVSKND VVDPVTEADK AHLLDYLRKM HGGGGGETGK
     TKITITRKQT GEIRKTDSTG KSRTIQVEVR KSRTYVKRDP AALAAEALAA AEPAAAAPAA
     PPPALEEVPA EPAPIEAQAP VAETPAAEPA VVEAPAPEPA VTAEVTAPAP VEAAPEPAPA
     AKPEGEAAPV KKTTRIKKAS ILNEAEVKAR EDEARRHQAL LERQAADAKA RIEREALRKQ
     AEAAREAAKL AEAQKAAAPA PAAPTEKTLH KPDKPAAAKG AKGPDKKPAG AWKDDAARRR
     GGLKTRGGAA PDAGWRGRKG KSKSGQEETT FVAPTEPIVR EVLVPETITV AELAHKMSVK
     AAEVIKALMK LGSMVTINQV LDQETAIIVV EEMGHIGKPA ALDTPEAFLI ETGEPGEAEM
     VARPPVVTVM GHVDHGKTSL LDTIRRTRVA SGEAGGITQH IGAYHVETEK GVITFLDTPG
     HEAFTAMRAR GAKATDIVVL VVAADDGVMP QTIEAIHHAK AAGVPLVVAV NKIDKPDANP
     ERIRQELVAQ GVTPEEWGGD TQFVEVSAKA NTNINGLLDA ILLQAEVLEL QAPADGPAKG
     IVIEARLDKG KGPVATLLVQ SGTLRRGDMV LAGQVYGRVR AMLDEAGKTV TEAGPSIPVE
     IQGLSDVPQA GEDMMVLPDE RKAREIALFR QGKYRDVQLA KKQAAKLESM FDQMGQGEVQ
     HLPIILKADM QGSYEGLAHA LGKISTDEVK VNIIHSGVGA ITESDVNLAL ASKAVLIGFN
     VRADASARKL AESSGVDIRY YNIIYEAVDE VKAALSGMLA PEKKESVIGT VEVRQVFVIS
     KVGTIAGCYV TDGVVKRGAG VRLIRNNVVI HQGELDSLKR FKDDVKEVKA NFECGLSLKN
     FNDIQEGDIL EVFEVVEVAR SL
 
 
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