IF2_ENT38
ID IF2_ENT38 Reviewed; 898 AA.
AC A4WEY3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ent638_3605;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP62263.1; -; Genomic_DNA.
DR RefSeq; WP_015960588.1; NC_009436.1.
DR AlphaFoldDB; A4WEY3; -.
DR SMR; A4WEY3; -.
DR STRING; 399742.Ent638_3605; -.
DR EnsemblBacteria; ABP62263; ABP62263; Ent638_3605.
DR KEGG; ent:Ent638_3605; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000230; 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.
FT CHAIN 1..898
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057656"
FT DOMAIN 397..566
FT /note="tr-type G"
FT REGION 51..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..413
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 431..435
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 542..544
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 506..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 898 AA; 97985 MW; 80DA04D7E8D6A452 CRC64;
MTDVTVKSLA TEIQTPVERL VQQFADAGIP KAADDSVTAQ EKQTLLAHLN REHGSTPDKL
TLQRKTRSTL SIPGTGGKSK SVQIEVRKTR TFVKRDPQEA ERLAAEEQAQ REAEEQAQRE
AVETAKREAV LKAEREAAEK AKRDANDKAK RDAAEKDKVS NQQTDEMTKT AQTEKARREN
EAAELKRKAE EEARRKLEED ARRVAEEARR MAEENAGVWA EQEKAKGEED KTDYHVTTSQ
HARQAEDEND REVEGNRSRT RTATKAARPQ KKGNKHAESK ADREEARAAG RGGKGGKRKG
SSLQQGFQKP AQAVNRDVVI GETITVGDLA NKMAVKGSQV IKAMMKLGAM ATINQVIDQE
TAQLVAEEMG HKVTLRRENE LEEAVMSDRD TGAAAESRAP VVTIMGHVDH GKTSLLDYIR
STKVASGEAG GITQHIGAYH VETDNGMITF LDTPGHAAFT SMRARGAQAT DIVVLVVAAD
DGVMPQTIEA IQHAKAAQVP VVVAVNKIDK PEADMDRVKT ELSQYGVMPE EWGGESQFIP
VSAKAGTGID DLLNAILLQA EVLELKAVRN GMASGAVIES FLDKGRGPVA TVLVREGTLN
KGDIVLCGFE YGRVRAMRNE LGQEVLEAGP SIPVEILGLS GVPAAGDEVT VVRDEKKARE
VALYRQGKFR EVKLARQQKS KLENMFANMT DGEVHEVNVV LKADVQGSVE AISDSLLKLS
TDEVKVKIIG SGVGGITETD ATLAAASNAI LVGFNVRADA SARKVIDSES LDLRYYSVIY
HLIDEVKAAM SGMLSPELKQ QIIGLAEVRD VFKSPKFGAI AGCMVTEGTI KRHNPIRVLR
DNVVIYEGEL ESLRRFKDDV NEVRNGMECG IGVKNYNDVR VGDMIEVFEI IEIQRSIA
