IF2_PROVU
ID IF2_PROVU Reviewed; 917 AA.
AC Q9ZF22;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PvuAU9201;
RA Steffensen S.A.D.A., Soballe B., Kristensen T., Mortensen K.K.,
RA Sperling-Petersen H.U.;
RT "Sequence of the infB gene from Proteus vulgaris.";
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=2;
CC Name=Alpha;
CC IsoId=Q9ZF22-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9ZF22-2; Sequence=VSP_018764, VSP_018765;
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; AJ002737; CAA05708.1; -; Genomic_DNA.
DR EMBL; AJ002737; CAA05709.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZF22; -.
DR SMR; Q9ZF22; -.
DR PRIDE; Q9ZF22; -.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000014472"
FT DOMAIN 416..585
FT /note="tr-type G"
FT REGION 102..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..432
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 450..454
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 471..474
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 525..528
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 561..563
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 102..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 471..475
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 525..528
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..181
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018764"
FT VAR_SEQ 182
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018765"
SQ SEQUENCE 917 AA; 101296 MW; 691DDDDD2C20D905 CRC64;
MTDETVKSLA EEIQTPVERL VQQFADAGIE KTVSDSVSQK EKETLLAWLN RDKDISTGQP
SKLTLQRKVR STLSVPGTGG KSKSVAIEVR KKRTYVNRDV IEKSQAEEQA LREAEEKAHR
EVEEKAQREA QEKAQRAAEE KAKREAQEAK KQAEEKAKRE AEEAKREAAE LAKREAAEKN
KVKQNDKPKA DVADQDKARR NAELAELKRK TEEAQRLKVE EETRAAAEKA RRLAEENAEK
WTAEPKAPET ESADYHVTTS RYARDAEDES DAEVEGDRRR GRTAKAPRAK KNNRHSEKAD
REEARAAGRS NKKGKRKSST LQQGFHKPAV AVNRDVIIGE TISVAELANK MAVKGSEVIK
TMMKMGAMAT INQVLDQETA QLVAEEMGHK VILRRENELE EQVMNDRDTG EESEVSRAPV
VTIMGHVDHG KTSLLDYIRS TKVASGEAGG ITQHIGAYHV KTDKGEITFL DTPGHAAFTS
MRARGAQVTD IVVLVVAADD GVMPQTIEAI QHAKAANVPV VVAVNKIDKH EADPDRVKTE
LSQYGILSED WGGETQFMHV SAKQGLGIDE LLDAILLQAE VLELKAVKEG MASGVVIESY
LDKGRGPVAT ILVREGTLNK GDIVLCGFEY GRIRAMRNEL GQEVQSAGPS MPVEILGLSN
VPSAGDEATV VRDEKKAREV ALYRQGKFRE VKLARQQKSK LENMFANMEE GKVSELNIVL
KTDVQGTCEA ITDALVKLST DEVKLRIIGS GVGGITETDA TLAAASEAII LGFNVRADAS
ARRIIEQESV DLRYYSVIYS LIDEIKLAMS GMLAPEYKQE IMGLAEVRDV FKSPKFGAVA
GCMVVEGNIK RNNPIRVLRD NVVIYEGELE SLRRFKDDVN EVRNGMECGI GVKNYNDVRV
GDMIEVFQVI EIKRSIA
