IF2_FLAPJ
ID IF2_FLAPJ Reviewed; 967 AA.
AC A6GWV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FP0470;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL42581.1; -; Genomic_DNA.
DR RefSeq; WP_011962639.1; NC_009613.3.
DR RefSeq; YP_001295399.1; NC_009613.3.
DR AlphaFoldDB; A6GWV8; -.
DR SMR; A6GWV8; -.
DR STRING; 402612.FP0470; -.
DR EnsemblBacteria; CAL42581; CAL42581; FP0470.
DR GeneID; 66551608; -.
DR KEGG; fps:FP0470; -.
DR PATRIC; fig|402612.5.peg.485; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; VIFAMNK; -.
DR Proteomes; UP000006394; 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; 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; PF04760; IF2_N; 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..967
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335469"
FT DOMAIN 465..635
FT /note="tr-type G"
FT REGION 201..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..481
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 499..503
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 521..524
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 575..578
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 611..613
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 230..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 521..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 575..578
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 967 AA; 105717 MW; 58C8505504C82266 CRC64;
MSEGTIRINK VLREFNISLE RAVDYLKDKG HVIESNPNTK ISDEVYNVLS NQFAGDKGNK
DASKEVGEEK RKEKEALRVE RENEIEEKRK VDEERQRQEV IRAKAVVTGL KQVGTIDLSA
KSVIKPTIIP GVKAEAKAEV KTEAKVEAKT EVKVEVKVEP KAEMPVAKTP EKSEQPKQHV
AKETLVKEKI FAKEPAKNVA KPIVGKTPEA TSKPSVEDAP VDETHETKYT KLTGPTFSGQ
TIDLSQFNKP KKIIEPNKGG AKPAGAGNNN NNKNKRKRIP TKSGEANATP RVPGTNLIRP
NTGGNATGGG FNRANKPGFV KGARPAIVPK VEPTEEDVKN QIKETLERLQ GKGNKSKAAK
YRRDKRDTHR QKSDDEQREL EAGSKTIKVT EFVTVGEVAT MMDVPITKVI GTCMSLGIMV
TMNQRLDAET LTIVCDEFGF EVEFITTDLE ENIEVVEDSA EDLVHRAPIV TVMGHVDHGK
TSLLDYIRKT NVIAGESGGI TQHIGAYGVE LENGQKIAFL DTPGHEAFTA MRARGAQVTD
IAIIVVAADD DIMPQTKEAI SHAQAANVPI IFAINKVDKQ NANPEKIKEK LAAMNFLVED
WGGKYQSQDI SAKTGIGMKE LLEKVLLEAE VLDLKANPNK PATGTVVEAF LDKGRGYVST
VLVQAGTMRV GDYILAGKNH GKIKAMQDER GNNVTEAGPS TPISILGLAG APTAGDKFNI
FADEREAKAI AAKRTQLMRE QSVRVQRHIT LDEIGRRIAL GQFKELNIIL KGDVDGSVEA
LSDSFSKLST PEIQINIIHK GVGAITETDV MLASASDAII IGFNVRPAGN AKQLAEKEEI
DIRHYSIIYA AIDDLRDAME GMLSPEMKEE ITGLAGVREL FKISKVGTIA GCMITDGKIL
RANKVRVIRD NVVIHTGDII ALKRFKDDVK EVAKGYDCGI QIKGFNEIEI DDIIEGFTEV
AVKRKLK
