IF2_ENTFA
ID IF2_ENTFA Reviewed; 798 AA.
AC Q835U8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=EF_1274;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016830; AAO81067.1; -; Genomic_DNA.
DR RefSeq; NP_814997.1; NC_004668.1.
DR RefSeq; WP_002357859.1; NZ_KE136528.1.
DR AlphaFoldDB; Q835U8; -.
DR SMR; Q835U8; -.
DR STRING; 226185.EF_1274; -.
DR PRIDE; Q835U8; -.
DR EnsemblBacteria; AAO81067; AAO81067; EF_1274.
DR KEGG; efa:EF1274; -.
DR PATRIC; fig|226185.45.peg.2228; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001415; 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; 2.
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..798
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137202"
FT DOMAIN 300..469
FT /note="tr-type G"
FT REGION 40..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..316
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 334..338
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 355..358
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 409..412
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 445..447
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 355..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 409..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 798 AA; 88147 MW; 36997A6EC01CE9CE CRC64;
MGKKRIYELA KEMNKASKDV VDKAHQLGMD VKNHMGAISS EQETKLRQAF GGGSTVNTQS
KATNNQKQQT TQNKPANKKP MNNKPGEQRN NQNRPNNQST NGQQRNNNNQ NRHGQSNTQN
RSNQTNTNNQ NRNTQNNNGS TTNQNRTSQN NNGGNNQNRG GQNRNNNFGG GQNRNNRNNF
NNQNRNRFNK KGKKGKHQQE SAKPAVPARK FRELPDVLEY TEGMNVADIA KKIHREPAEI
IKKLFMMGVM VNQNQALDKD TIELLAVDYG MEPQEKVQVD IADIDKFFEP EAVVEENLTT
RPPVVTIMGH VDHGKTTLLD TLRHSRVTSG EAGGITQHIG AYQLDIDGKP ITFLDTPGHA
AFTSMRARGA SITDITILVV AADDGVMPQT IEAINHAKAA KVPIIVAVNK IDKPGANPDH
VKQELSEHEL IPEEWGGDTI FVNISAKFNQ NIDELLENIL LIAEVEDLKA DPTQKAIGTV
IEARLDKGKG PVATLLVQQG TLHVGDPIVV GNTYGRVRVM TNDMGRRDKE AGPATPVEIT
GLNDVPQAGD RFVVFEDEKT ARQAGEERAK RALLEQRSAS SRVTLDNLFE SLKEGELKEV
NIIVKADVQG SAEAVSASLQ KIDVEGVRVK IVHAAVGAIN ESDVTLAAAS NAIIIGFNVR
PTPQAKQQAE QEEVDIRLHR IIYKALEEIE TAMKGLLDPE FEEKITGQMT VRELYKVSKV
GTIAGCYVTE GFIRRDSGVR VIRDGIVIYE GKLASLKRFK DDVKEVKLGF ECGAMIENFN
DLRVDDAIEG FIMEEIKQ
