IF2_PSEA8
ID IF2_PSEA8 Reviewed; 840 AA.
AC B7V1F6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PLES_51291;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
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; FM209186; CAW29883.1; -; Genomic_DNA.
DR RefSeq; WP_003095190.1; NC_011770.1.
DR AlphaFoldDB; B7V1F6; -.
DR SMR; B7V1F6; -.
DR KEGG; pag:PLES_51291; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
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.
FT CHAIN 1..840
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117335"
FT DOMAIN 340..509
FT /note="tr-type G"
FT REGION 95..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..356
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 374..378
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 395..398
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 449..452
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 485..487
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 95..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 395..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 449..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 840 AA; 90884 MW; 85BA662DD51CDE3D CRC64;
MTQVTVKELA QVVDTPVERL LLQMRDAGLP HTSAEQVVTD SEKQALLTHL KGSHGDRASE
PRKITLQRKT TTTLKVGGSK TVSVEVRKKK TYVKRSPDEI EAERQRELEE QRAAEEAERL
KAEEAAARQR AEEEARKAEE AARAKAAQEA AATAGAEPAV VADVAVAEPV AKPAAVEERK
KEEPRRAPKR DEDDDRRDRK HTQHRPSVKE KEKVPAPRVA PRSTDEESDG YRRGGRGGKS
KLKKRNQHGF QNPTGPIVRE VNIGETITVA ELAAQMSVKG AEVVKFMFKM GSPVTINQVL
DQETAQLVAE ELGHKVKLVS ENALEEQLAE SLKFEGEAVT RAPVVTVMGH VDHGKTSLLD
YIRRAKVAAG EAGGITQHIG AYHVETERGM VTFLDTPGHA AFTAMRARGA QATDIVILVV
AADDGVMPQT QEAVQHAKAA GVPIVVAVNK IDKPEANPDN IKNGLAALDV IPEEWGGDAP
FVPVSAKLGT GVDELLEAVL LQAEVLELKA TPSAPGRGVV VESRLDKGRG PVATVLVQDG
TLRQGDMVLV GINYGRVRAM LDENGKPIKE AGPSIPVEIL GLDGTPDAGD EMTVVADEKK
AREVALFRQG KFREVKLARA HAGKLENIFE NMGQEEKKTL NIVLKADVRG SLEALQGSLS
GLGNDEVQVR VVGGGVGGIT ESDANLALAS NAVLFGFNVR ADAGARKIVE AEGLDMRYYN
VIYDIIEDVK KALTGMLGSD LRENILGIAE VRDVFRSPKF GAIAGCMVTE GMVHRNRPIR
VLRDDVVIFE GELESLRRFK DDVAEVRAGM ECGIGVKSYN DVKVGDKIEV FEKVEVARSL
