IF2_NITWN
ID IF2_NITWN Reviewed; 871 AA.
AC Q3SWP9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Nwi_0024;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA03292.1; -; Genomic_DNA.
DR RefSeq; WP_011313363.1; NC_007406.1.
DR AlphaFoldDB; Q3SWP9; -.
DR SMR; Q3SWP9; -.
DR STRING; 323098.Nwi_0024; -.
DR EnsemblBacteria; ABA03292; ABA03292; Nwi_0024.
DR KEGG; nwi:Nwi_0024; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002531; 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; 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; 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..871
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228217"
FT DOMAIN 367..538
FT /note="tr-type G"
FT REGION 1..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..383
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 401..405
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 424..427
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 478..481
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 514..516
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376..383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 424..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 871 AA; 93665 MW; A6B619F436A55F2B CRC64;
MVDTKNPGDK TLSVSPTKTL TLKPRVEQGT VRQSFSHGRT KQVVVEKRGK RRIGGDSPGP
EPAGTSEPAS ARTPAAKAPP ARAATPAAPR AGSGVVLRKL TEDERSARAS ALAEAKVRAE
EERRIAEAEA ARRNSKEGIE QAEREAAEAR RKAEEERHRQ EEEAKRKAEI EAKRRFGQTE
SKPAPAKTTT TTTRAAPPAR PAAVAADGSD EDEAPRLVRR PGGPARPVIA PKPAAKPAPA
KQRGRLTLVT ALSADDVRER SIASFRRRTQ RLKGHASNEP KEKLVREVVV PEAITIQELA
NRMAERAVDV IRMLMKQGAM HKITDVIDAD TAQLIAEELG HTVKRVAASD VEEGLFDVVD
NSTDIEPRSP VVTVMGHVDH GKTSLLDALR HANVVSGEAG GITQHIGAYQ VTSPESGKKI
TFIDTPGHAA FTAMRARGAK VTDLVILVVA ADDGVMPQTI EAINHAKAAK VPMIIAINKI
DKPEAKPERV RTELLQHEVQ VESMGGQVVD VEVSAKNKTN LDKLLEMISL QADLLDLKTN
ASRPAEGTVI EAKLDRGRGP VATVLVQRGT LRVGDIIVAG AEMGRVRALI SDQGETVNEA
GPSVPVEVLG FNGPPEAGDR LAVVENEARA RQVTSYRAHQ KRENAAASTS GMRGSLEQMM
SQLKTVGRKD FPLIIKADVQ GSLEAILGSL EKLGTDEVAA RILHAGVGGI SESDVTLAEG
FNAAIIGFSV RANKEAAAAA KRNGIEIRYY NIIYDLVDDV KKAMSGLLAP TLRETMLGNA
EILEVFNISK VGKVAGCRVT DGSVERGANV RLIRDNVVVH EGKLSTLKRF KDEVKEVQSG
QECGMAFESY GDMRVGDVIE CYRVETIQRS L
