IF2_NITEU
ID IF2_NITEU Reviewed; 889 AA.
AC Q82WD0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NE0761;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(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}.
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DR EMBL; AL954747; CAD84672.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82WD0; -.
DR SMR; Q82WD0; -.
DR STRING; 228410.NE0761; -.
DR EnsemblBacteria; CAD84672; CAD84672; NE0761.
DR KEGG; neu:NE0761; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q82WD0; -.
DR Proteomes; UP000001416; 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..889
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137228"
FT DOMAIN 391..560
FT /note="tr-type G"
FT REGION 158..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..407
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 425..429
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 536..538
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 189..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 889 AA; 96987 MW; C214256F543034D3 CRC64;
MLMTQMTVEQ FAHDLGMLPG LLLEQLQAAG VDKRSAADFV TEQDKTRLLD YLRKSHGSSG
PRTRITLARK QTTEIKQSDS TGRPRTIEVK VKKTRVLTRQ NEPEVIEKSV SEEPAPLKMV
ETPEPTIVKS VVDAEQMALR AEEARKRSEL IARQAAELKE KQEKRRQQAA AQANVKKEPA
PAEQESGPAT AVTPGSVTEI SSKLPETGAA ATPATSTAPA TTSTTAATKG HAPQKPVVKP
EEKGEKKKKP TKQDAWKDEP VKRREPKARG DLSGGQEWRM RKDKHGKYKS DELQSQHAFS
VPTEPVIHEV LIPETISVGA LAQKMAVKAA EVIKVLMKMG SMVTINQMLD QETAMVVVEE
MGHIAKIAAS DNPESFLEEV DVSSDEARME PRAPVVTVMG HVDHGKTSLL DYIRRTRVAG
GEAGGITQHI GAYHVETSRG VITFLDTPGH EAFTAMRARG AKITDIVILV VAADDGVMPQ
TIEAIHHAKA ANIPIVVAVN KMDKPEANFD RIKQELVNHG VVPEDWGGDA MFIGVSAKTG
LGIDELLEAV LLQAEVLELK AVREAPAKGV VIESRLDKGR GPVATVLVQS GTLRRGDAVL
TGAVFGKIRA MLNERGKSIS EASTSIPVEI QGLSEVAVAG EVFIALDDER KAREIALFRQ
GKFRDVRLDK LQVAKMEDVF GQHEDVSTLN LIIKADVQGS CEALVYALKK LETDEVKINV
VHSGVGAIIE SDINLALASK AVVIGFNCRA DLGARKLITS TGVDVRYYNI IYEAVDEVKK
ALSGMMMPDR KEKILGMVDI REIYRISKVG VVAGCYVLEG LIKRDALVRL LRDGLVIHSG
SLDSLKRFKE DVREVKSGFE CGLSLKNFND IQQGDQIEVY EIVETARVL
