IF2_ENTCL
ID IF2_ENTCL Reviewed; 897 AA.
AC Q9ZF25;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB;
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EclAU9501;
RA Steffensen S.A.D.A., Poulsen A.B., Fage-Larsen J., Korsager B.,
RA Mortensen K.K., Sperling-Petersen H.U.;
RT "Sequence of the infB gene from Enterobacter cloacae.";
RL Submitted (NOV-1997) 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q9ZF25-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9ZF25-2; Sequence=VSP_018756, VSP_018757;
CC Name=Gamma;
CC IsoId=Q9ZF25-3; Sequence=VSP_018755;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ002736; CAA05703.1; -; Genomic_DNA.
DR EMBL; AJ002736; CAA05704.1; -; Genomic_DNA.
DR EMBL; AJ002736; CAA05705.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZF25; -.
DR SMR; Q9ZF25; -.
DR STRING; 1399774.JDWH01000009_gene1830; -.
DR eggNOG; COG0532; Bacteria.
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 Alternative initiation; Cytoplasm; GTP-binding; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..897
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000014466"
FT DOMAIN 396..565
FT /note="tr-type G"
FT REGION 52..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..412
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 430..434
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 451..454
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 505..508
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 541..543
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..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 451..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 505..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_018755"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018756"
FT VAR_SEQ 159
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018757"
SQ SEQUENCE 897 AA; 97893 MW; 5F66372D567798BA CRC64;
MTDVTVKTLA AEIQTSVDRL VQQFADAGIP KSADDSVTAQ EKQTLLSHLN REHGSAPDKL
TLQRKTRSTL NVPGTGGKSK SVQIEVRKTR TFVKRDPQEA ERLAAEEQAQ REAEEQAQRE
AEITAKREAE LKAEREAAEK AKRDASDKAK RDAAEKDKVS NQQTDEMTKT AQTEKARREN
EAAELKRKAE EEARRKLEED ARRVAEEARR MAEENEKNGI NPVEQTEDTS DYHVTTSQHA
RQAEDENDRE VEGGRGRTRT ASKTARPQKK GNKHAESKAD REEARAAGRG GKGGKRKGSP
LLQQGFQKPA QAVNRDVVIG ETITVGDLAN KMAVKGSQVI KAMMKLGAMA TINQVIDQET
AQLVAEEMGH KVILRRENEL EEAVMSDRDT GAAAEPRAPV VTIMGHVDHG KTSLLDYIRS
TKVASGEAGG ITQHIGAYHV ETDNGMITFL DTPGHAAFTS MRARGAQATD IVVLVVAADD
GVMPQTIEAI QHAKAAQVPL VVAVNKIDKP EADMDRVKNE LSQYGVMPEE WGGEAQFIPV
SAKAGTGIDD LLNAILLQAE VLELKAIRNG MASGAVIESF LDKGRGPVAT VLVREGTLNK
GDIVLCGFEY GRVRAMRNEL GQEVLEAGPS IPVEILGLSG VPAAGDEVTV VRDEKKAREV
ALYRQGKFRE VKLARQQKSK LENMFANMTE GEVHEVNVVL KADVQGSVEA ISDSLLKLST
DEVKVKIIGS GVGGITETDA TLAAASNAIL VGFNVRADAS ARKVIESESL DLRYYSVIYN
LIDEVKAAMS GMLSPELKQQ IIGLAEVRDV FKSPKFGAIA GCMVTEGNIK RHNPIRVLRD
NVVIYEGELE SLRRFKDDVN EVRNGMECGI GVKNYNDVRV GDMIEVFEII EIQRTIA
