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