IF2_POLNS
ID IF2_POLNS Reviewed; 917 AA.
AC B1XV89;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pnec_1093;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB44266.1; -; Genomic_DNA.
DR RefSeq; WP_012358029.1; NC_010531.1.
DR AlphaFoldDB; B1XV89; -.
DR SMR; B1XV89; -.
DR STRING; 452638.Pnec_1093; -.
DR PRIDE; B1XV89; -.
DR EnsemblBacteria; ACB44266; ACB44266; Pnec_1093.
DR KEGG; pne:Pnec_1093; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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.
FT CHAIN 1..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093810"
FT DOMAIN 415..582
FT /note="tr-type G"
FT REGION 241..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..431
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 449..453
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 560..562
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 241..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 917 AA; 97962 MW; 429B5DCCBEE3955C CRC64;
MATTVKVLAK ELKRTAPDLL EQLKAAGIEK GSEDDSITEK DKTVLLEHLQ KAHGSTDTGA
RKKITLIKRE SSEIRQADSA GRTRTVQVEV RKKRVLVKAG DKAPEEVAAQ PVKQVAPAAP
AKPVISEEEL EKRAAEATRQ AELLARQEAE MKAAEEARQK EVTVPVVKEV APVDKAPVAP
AVAEKKLAAD KAAKDLAASK EKELADIRAR RAAAEAEALA IRDMMSAPAR VLKAPSEVAA
EEAKKGTLHK PAKAEGAEDK KKAATKVGGK TIKSSETSST WQEEGTRKSG GLKTRGDTSG
GVGGWRSGGG RKKQRQIAEA NVDTNFQVPI EPVIRDVHVP ETITVAELAH AMAVKSAEVI
KLLMGMGQMV TINQVLDQDT AMIIVEEMGH KAHAAKLDDP DLDLGTEGHD AELLPRPPVV
TVMGHVDHGK TSLLDKIRTA KVAIGEVGGI TQHIGAYHVE TPRGMITFLD TPGHEAFTAM
RARGAKATDI VILVVAADDG VMPQTKEAIH HAIAGGVPLV VAINKIDKPE ANSERVKAEL
VAEQVVLEEY GGDVPFIPVS AKTGEGIDAL LENVLLQAEI LELKAPKEAP AQGLVIEARL
DKGKGPVATV LVQSGTLKRG DMLLAGSSFG RVRAMMDENG KPCNEAGPSI PVEIQGLSEV
PAAGEAVQVM PDERKAREIA LFRQGKFRDV KLAKQQAVKL ENMMETIGEG AIEAKLLPLI
IKADVQGSQE ALSQLLMKLS IPEVKVQIVH AAVGGITETD VNLAVVSKAV IIGFNSRADA
AARKLAENNG VDIRYHNIIY DAVDEVKLAL SGMLIPGKKE EITGLVEIRQ VFLVSKVGAI
AGCLVVDGIV KRTSSVRLLR DNVVVWTGEL DSLKRFKDDA KEVRAGVECG LSLKGYNDIK
EGDQLEVFEV TEVARSL
