IF2_TERTT
ID IF2_TERTT Reviewed; 940 AA.
AC C5BPV9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TERTU_3217;
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901;
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR14658.1; -; Genomic_DNA.
DR RefSeq; WP_015820772.1; NC_012997.1.
DR AlphaFoldDB; C5BPV9; -.
DR SMR; C5BPV9; -.
DR STRING; 377629.TERTU_3217; -.
DR PRIDE; C5BPV9; -.
DR EnsemblBacteria; ACR14658; ACR14658; TERTU_3217.
DR KEGG; ttu:TERTU_3217; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000009080; 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; 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; Reference proteome.
FT CHAIN 1..940
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202785"
FT DOMAIN 441..610
FT /note="tr-type G"
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..457
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 475..479
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 550..553
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 586..588
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 118..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 450..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 550..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 940 AA; 101496 MW; 4DBA95DBFA2AF6E0 CRC64;
MAEVTVSELA KSVGASVDRI LAQMKQAGLS HQTPDDTVSD EEKQTLLSFL KSSHGESAAA
PKKITLKRKT TTTLKTGSGS GRKTVNVEVR KKRTYVKREL TAEDATETAA DEVLIPEQEQ
LESTSVAEIP ESVSSDTAVE EIVADTVVEA EVEAASPEPE PEVEATPEPE VEDVVAEEAE
PAAAEPAPAP VVEQRSSFVD DAEILRQRAA VRKKAEEEAE VARRKADAEK AEAAAKQKAE
QAAVQKGSVE KPAAGDKDES KHHKKPKPKS ETEEFDEEAK AKHNKKAGKA VKKVAGPKKV
ASALDYVEDK EEIDEVIHSA PKSKKGGQNN NSSNSGSRPL IKVANRHGFK KPTGKITYKV
EIPEEIVVSE LAQRMNVKAG EVVKHLFKLG TMVTINQAID QETAQLVVEE MGHEAVLVSG
DAVEQKLREQ VVEVDDAELV ARAPVVTVMG HVDHGKTSLL DYIRKTRVAS GEAGGITQHI
GAYRVNTSHG ELAFLDTPGH AAFTAMRARG AQCTDVVILV VAADDGVMPQ TEEAVQHARA
AGVPLVVAVN KIDKEAADPD RVKNELSAKD VIPEDWGGDT QFINVSAQTG EGIEELLEAV
ALQAELLELS APVNVPARGV VIESRMDKGR GVVATVLVQG GELKRGDIML AGQSFGRVRA
MVNEYGDNID SAPPSTPVEI LGLDTPPEAG DEFLVVPDER KAREVSEFRA EKERTERMQR
QQAAKLENMF AGMGSDEKKI LPIVLKTDVR GSLEAIQAAL LDVGNDEVQV NFVGGGVGGI
TENDVNLALT SGAVIVGFNV RADNSARKLA ESESAEIRYY SIIYQLIDEV KSALAGMLDP
ERVEEIVGIA EVRDVFRSPK FGQVAGCMVV EGNVYRNKPI RVLRDNVVIF EGELESLRRF
KDDVNEVRNG MECGIGVKNY DVKVGDQIEV FDVKEVAREL
