IF2_NITEC
ID IF2_NITEC Reviewed; 888 AA.
AC Q0AFJ3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Neut_1646;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59889.1; -; Genomic_DNA.
DR RefSeq; WP_011634695.1; NC_008344.1.
DR AlphaFoldDB; Q0AFJ3; -.
DR SMR; Q0AFJ3; -.
DR STRING; 335283.Neut_1646; -.
DR PRIDE; Q0AFJ3; -.
DR EnsemblBacteria; ABI59889; ABI59889; Neut_1646.
DR KEGG; net:Neut_1646; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001966; 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.
FT CHAIN 1..888
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057659"
FT DOMAIN 390..559
FT /note="tr-type G"
FT REGION 96..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..406
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 424..428
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 499..502
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 535..537
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 96..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 499..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 888 AA; 96697 MW; 1F73FD811BC59AC6 CRC64;
MTQMTVEQFA HDLGMLPNLL LEQLQAAGVA KRSAADFVTE QDKTQLLDYL RKSHGSSGSR
TKITLARRQT TEIKQSDSAG RPRTIEVKVR KKRVLTTKQD ESDAAGKRAA EDVSLRTAEA
PEAPEAVPVK SVLDAEQIAL RAEEARKRSE LMARQAAELK EKQEKRRQQV TAQTEVKKES
TQVQEPGSET AAVSGSVAAT QPESTETAAV TPSATITVTT QTTPAAKERA PQKPAVKPEE
KGEKKKKQAR QQEAWKDEPV KRRESKARGD VSGGQEWRMR KDKHGRSRSD ESQSQHAFSA
PTEPVVHEVL IPETISVAVL AQKMAVKAAE VIKVLMKMGN MVTINQMLDQ DTAMIVVEEM
GHVAKIAAPD NPEAFLEEVD LSPDEARMES RAPVVTVMGH VDHGKTSLLD YIRRTRVAGG
EAGGITQHIG AYHVKTSRGV VTFLDTPGHE AFTAMRARGA KITDIVILVV AADDGVMPQT
IEAVHHAKAA SIPIVVAVNK MDKPEANLER IKQELVNHGV VPEDWGGDAM FIGVSAKTGQ
GIDELLEAVL LQAEVLELKA VRDAPAKGVI IESRLDKGRG PVATVLVQSG TLRRGDVVLT
GAVFGKIRAM LDERGKSVSE AGTSIPVEIQ GLSEVAAAGE VFIALSDERK AREIALFRQG
KFRDVRLDKL HVAKMEDVFG HQEDISTLNL IIKADVQGSC EALAYALKKL ETDEVKINIV
HSGVGAIIES DINLALASKA VVIGFNCRAD LGARKLIAST GVDVRYYNII YEAVDEVKKA
LSGMMTPDRK EKILGLVDIR EIYRISKVGV VAGCYVLEGL IRRDAPVRVL RDGVVIHSGS
LDSLKRFKDD VKEVKSGFEC GLSLKNFNDI QQGDQIEVYE IVETARVL
