IF2_PSEAB
ID IF2_PSEAB Reviewed; 840 AA.
AC Q02FS8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PA14_62760;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ14127.1; -; Genomic_DNA.
DR RefSeq; WP_003100517.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02FS8; -.
DR SMR; Q02FS8; -.
DR PRIDE; Q02FS8; -.
DR EnsemblBacteria; ABJ14127; ABJ14127; PA14_62760.
DR KEGG; pau:PA14_62760; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR BioCyc; PAER208963:G1G74-5307-MON; -.
DR Proteomes; UP000000653; 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.
FT CHAIN 1..840
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008303"
FT DOMAIN 340..509
FT /note="tr-type G"
FT REGION 94..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..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 94..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; 90856 MW; 9428C38AC50A7495 CRC64;
MTQVTVKELA QVVDTPVERL LLQMRDAGLP HTSAEQVVTD SEKQALLTHL KGSHGDRASE
PRKITLQRKT TTTLKVGGSK TVSVEVRKKK TYVKRSPDEI EAERQRELEE QRAAEEAERL
KAEEAAARQR AEEEARKAEE AARAKAAQEA AATAGAEPAV VADVAAAEPV 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
