IF2_PSEPW
ID IF2_PSEPW Reviewed; 843 AA.
AC B1J2A9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=PputW619_0721;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA71226.1; -; Genomic_DNA.
DR RefSeq; WP_012312654.1; NC_010501.1.
DR AlphaFoldDB; B1J2A9; -.
DR SMR; B1J2A9; -.
DR STRING; 390235.PputW619_0721; -.
DR PRIDE; B1J2A9; -.
DR EnsemblBacteria; ACA71226; ACA71226; PputW619_0721.
DR KEGG; ppw:PputW619_0721; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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..843
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093815"
FT DOMAIN 343..516
FT /note="tr-type G"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 91174 MW; E38AA179F5B8C452 CRC64;
MTQVTVKELA QEVEAPVERL LQQMREAGLP HTDAGQVVTD NEKQTLLTHL KSSHKSKAEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI QAEQKREQDE RRAAENAARD
KVDADVRQRN EEQARRHATA TAAAAPAAKA EPAPAAAAPA PAPVVADAPA SEDAAARAAE
RKKDETRRNE SRTRDDDRRR GEAPRVSIKV KVKEKEKAPT PRAAPRTTDE ESDGARRGRG
GKGKLKKRNQ HGFQNPTGPV IRDVTIGETI TVSELAQQMS VKAAEVVKFM FKMGTPVTIN
QVLDQETAQL IAEELGHKVT LVSDTALEDS LAESLKFEGQ AESRAPVVTV MGHVDHGKTS
LLDYIRRAKV AAGEAGGITQ HIGAYHVETD RGMVTFLDTP GHAAFTQMRA RGAKATDIVI
LVVAADDGVM PQTREAVQHA KAAGVPLVVA VNKIDKPGAD LDRIRNELSV EGVTSEEWGG
DTPFVKVSAK MGTGVDELLE AVLLQAEVLE LTATPTAPGR GVVVESRLDK GRGPVATILV
QDGTLRQGDM VLCGSNYGRV RAMLDENGKP VKEAGPSIPV EILGLDGTPE AGDELSVVAD
EKKAREVALF RQGKYREVKL ARAHAGKLEN IFETMGQEEK KTLNIVLKTD VRGSLEALQG
SLGGLGNDEV QVRVIGGGVG GITESDANLA LASNAVLFGF NVRADAGARK IVEQEGLDMR
YYNVIYDIIE DVKKALTGML GSDVRENILG VAEVRDVFRS PKFGAIAGCM VIEGTVYRNR
PIRVLRDDVV IFEGELESLR RFKDDAAEVR SGMECGIGVK SYNDVKVGDK IEVFEKVQVA
RTL
