IF2_PSEPK
ID IF2_PSEPK Reviewed; 846 AA.
AC Q88DV7;
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=PP_4712;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70284.1; -; Genomic_DNA.
DR RefSeq; NP_746820.1; NC_002947.4.
DR RefSeq; WP_003249965.1; NC_002947.4.
DR AlphaFoldDB; Q88DV7; -.
DR SMR; Q88DV7; -.
DR STRING; 160488.PP_4712; -.
DR EnsemblBacteria; AAN70284; AAN70284; PP_4712.
DR KEGG; ppu:PP_4712; -.
DR PATRIC; fig|160488.4.peg.5022; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q88DV7; -.
DR BioCyc; PPUT160488:G1G01-5035-MON; -.
DR Proteomes; UP000000556; 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; Reference proteome.
FT CHAIN 1..846
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137237"
FT DOMAIN 346..513
FT /note="tr-type G"
FT REGION 94..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..362
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 380..384
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 401..404
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 491..493
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 401..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 846 AA; 91461 MW; 20ABE2468CAFE4A8 CRC64;
MTQVTVKELA QEVEAPVERL LQQMREAGLP HTDAGQVVTD NEKQTLLTHL KSSHKSKAEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI QAEQKRELDE RRAAENAARD
KVEAEVRQRN EEQARRQAAG SAAAAPAPAA KPEPAPAAAP VAAPAPVVAD APASEDAAAR
AAERKKDETR RNESRTRDDD RRRGEAPRVS IKVKVKEKEK APTPRAAPRT TDEESDGARR
GRGGKSKLKK RNQHGFQNPT GPVIRDVTIG ETITVSELAN QMSVKGAEVV KFMFKMGTPV
TINQVLDQET AQLIAEELGH KVTLVSDTAL EDSLAESLKF EGQTESRAPV VTVMGHVDHG
KTSLLDYIRR AKVAAGEAGG ITQHIGAYHV ETDRGMVTFL DTPGHAAFTQ MRARGAKATD
IVILVVAADD GVMPQTREAV QHAKAAGVPL VVAVNKIDKP GADLDRIRNE LSVEGVTSED
WGGDTPFVKV SAKMGTGVDE LLEAVLLQAE ILELTATPTA PGRGVVVESR LDKGRGPVAT
ILVQDGTLRQ GDMVLCGSNY GRVRAMLDEN GKPVKEAGPS IPVEILGLDG TPEAGDELSV
VADEKKAREV ALFRQGKYRE VKLARAHAGK LENIFETMGQ EEKKTLNIVL KTDVRGSLEA
LQGSLGGLGN DEVQVRVIGG GVGGITESDA NLALASNAVL FGFNVRADAG ARKIVEQEGL
DMRYYNVIYD IIEDVKKALT GMLGSDVREN ILGVAEVRDV FRSPKFGAIA GCMVIEGTVY
RNRPIRVLRD DVVIFEGELE SLRRFKDDAS EVRSGMECGI GVKSYNDVKV GDKIEVFEKV
QVARTL
