IF2_PSEFS
ID IF2_PSEFS Reviewed; 841 AA.
AC C3K259;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PFLU_5253;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM181176; CAY52351.1; -; Genomic_DNA.
DR RefSeq; WP_015885918.1; NC_012660.1.
DR AlphaFoldDB; C3K259; -.
DR SMR; C3K259; -.
DR STRING; 294.SRM1_00826; -.
DR PRIDE; C3K259; -.
DR EnsemblBacteria; CAY52351; CAY52351; PFLU_5253.
DR KEGG; pfs:PFLU_5253; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002332; 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..841
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202782"
FT DOMAIN 341..510
FT /note="tr-type G"
FT REGION 94..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..357
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 375..379
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 396..399
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 486..488
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350..357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 841 AA; 90599 MW; 3E13B60B045DEE85 CRC64;
MTQVTVKQLA DEVKTPVERL LQQMREAGLP HTAADEGVSD SEKQSLLTHL KSSHKAKVEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI EAERKRELEE RRAVENAARQ
KAEEEAKRRA EEEARRQPAA AQPAGTEAVA APVAPVEAVR EAAPVAAAPA PAADARKRDE
PRRPDKPRAD DNNRRGGGGD GERKNAPHRA SVKEKAPAPR VAPRTTDEES DGFRRGGRGK
AKLKKRNAHG FQSPTGPVVR DVQIGETITV GDLANQMSVK AAEIIKFMFK LGTPATINQV
LDQETAQLVA EELGHKVTLV SDTALEDSLA ESLKFEGETF SRAPVVTVMG HVDHGKTSLL
DYIRRAKVAA GEAGGITQHI GAYHVETERG MVTFLDTPGH AAFTAMRARG AKATDIVILV
VAADDGVMPQ TIEAVQHAKA AGVPLVVAVN KIDKPGADLD RIRSELSVHG VTSEEWGGDT
PFVSVSAKVG TGVDELLEAV LLQAEVLELK ATPSAPGRGV VVESRLDKGR GPVATVLVQD
GTLRQGDMVL VGSNYGRVRA MLDENGKPIK EAGPSIPVEI LGLDGTPDAG DEMSVLSDEK
KAREVALFRQ GKFREVKLAR AHAGKLENIF ENMGQAEKKT LNIVLKSDVR GSLEALNGAL
NGLGNDEVQV RVVGGGVGGI TESDANLALA SNAVLFGFNV RADAGARKIV EQEGLDMRYY
NVIYDIIEDV KKALTGMLGS DVRENILGVA EVRDVFRSPK FGAIAGCMVI EGTVYRNRPI
RVLREDIVIF EGELESLRRF KDDASEVRAG MECGIGVKSY NDVKAGDKIE VYEKVQVARS
L
