IF2_PSEF5
ID IF2_PSEF5 Reviewed; 838 AA.
AC Q4KIF6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PFL_0844;
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY96242.1; -; Genomic_DNA.
DR RefSeq; WP_011059202.1; NC_004129.6.
DR AlphaFoldDB; Q4KIF6; -.
DR SMR; Q4KIF6; -.
DR STRING; 220664.PFL_0844; -.
DR PRIDE; Q4KIF6; -.
DR EnsemblBacteria; AAY96242; AAY96242; PFL_0844.
DR GeneID; 57473845; -.
DR KEGG; pfl:PFL_0844; -.
DR PATRIC; fig|220664.5.peg.864; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008540; 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; Reference proteome.
FT CHAIN 1..838
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228229"
FT DOMAIN 338..507
FT /note="tr-type G"
FT REGION 30..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..354
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 372..376
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 393..396
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 447..450
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 483..485
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347..354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 393..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 447..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 838 AA; 90500 MW; D5FCA72F7DA1B8BC CRC64;
MTQVTVKQLA DEVKTPVERL LQQMREAGLP HTAAEEHVSD SEKQSLLTHL KSSHKAKVEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI EAERQRELEE RRAVENAARQ
KAEEEAKRRA EEEARRQPAP VAEPVAAQAA APAPAPVVEP VQEAPVATAA PAADARKKDE
QRRPDKTRND DNRRGGDGER KNAPHRASVK EKAPAPRVAP RTTDEESDGF RRGGRGKAKL
KKRNAHGFQS PTGPVVRDVQ IGETITVGEL AQQMSVKAAE VIKFMFKLGT PATINQVLDQ
ETAQLVAEEL GHKVTLVSDT ALEDSLAESL KFEGEAVARA PVVTVMGHVD HGKTSLLDYI
RRAKVAAGEA GGITQHIGAY HVETERGMVT FLDTPGHAAF TAMRARGAKA TDIVILVVAA
DDGVMPQTVE AVQHAQAAGV PLVVAVNKID KPGADLDRIR SELSVHGVTS EDWGGDTPFV
PVSAKMGTGV DDLLEAVLLQ AEVLELKATP SAPGRGVVVE SRLDKGRGPV ATVLVQDGTL
RQGDMVLVGS NYGRVRAMLD ENGKPIKEAG PSIPVEILGL DGTPDAGDEM SVVADEKKAR
EVALFRQGKF REVKLARAHA GKLENIFESM GQEEKKTLNI VLKSDVRGSL EALQGALNGL
GNDEVQVRVV GGGVGGITES DANLALASNA VLFGFNVRAD AGARKIVEQE GLDMRYYNVI
YDIIEDVKKA LTGMLGSDVR ENILGVAEVR DVFRSPKFGA IAGCMVIEGV VHRNRPIRVL
REDIVIFEGE LESLRRFKDD ASEVRAGMEC GIGVKSYNDV KVGDKIEVFE KVQVARSL
