IF2_KLEOX
ID IF2_KLEOX Reviewed; 896 AA.
AC Q9ZF28;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KoxAU9501;
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 Klebsiella oxytoca.";
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=Q9ZF28-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9ZF28-2; Sequence=VSP_018761, VSP_018762;
CC Name=Gamma;
CC IsoId=Q9ZF28-3; Sequence=VSP_018763;
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; AJ002735; CAA05698.1; -; Genomic_DNA.
DR EMBL; AJ002735; CAA05699.1; -; Genomic_DNA.
DR EMBL; AJ002735; CAA05700.1; -; Genomic_DNA.
DR RefSeq; WP_025108147.1; NZ_CP026285.1.
DR AlphaFoldDB; Q9ZF28; -.
DR SMR; Q9ZF28; -.
DR STRING; 571.MC52_05130; -.
DR GeneID; 66557643; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 347113at2; -.
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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000014469"
FT DOMAIN 395..564
FT /note="tr-type G"
FT REGION 94..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..411
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 429..433
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 504..507
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 540..542
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..228
FT /note="Basic and acidic 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 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 450..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 504..507
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_018763"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018761"
FT VAR_SEQ 159
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018762"
SQ SEQUENCE 896 AA; 98095 MW; C1EB16F88FE39B6D CRC64;
MTDVTIKALA SEIQTSVDRL IQQFADAGIR KSADDSVTAQ EKQTLLTHLN REHGSAPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEAAKREAQ LKAEREAAEQ AKRELADKAK REAAEKDKVS NQQTDDMTKT AQAEKQRREN
EAAELKRKSE EEARRKLEEE ARRVAEEARR MAQENEKNWT EAPETPEETT DYHVTTSQHA
RQAEDDNDRE VEGGRGRGRN AKAARPAKKG NKHAESKADR EEARAAVRGG KGGKHRKGSA
LQQGFQKPAQ AVNRDVIIGE TITVGDLANK MAVKGSQVIK AMMKLGAMAT INQVIDQETA
QLVAEEMGHK VILRRENELE EAVMSDRDTG AAAEPRAPVV TIMGHVDHGK TSLLDYIRST
KVASGEAGGI TQHIGAYHVE TDNGMITFLD TPGHAAFTSM RARGAQATDI VVLVVAADDG
VMPQTIEAIQ HAKAAQVPLV VAVNKIDKPE ADLDRVKNEL SQYGVMPEEW GGEAQFIPVS
AKAGTGIDDL LNAILLQAEV LELKAVRNGM ASGAVIESFL DKGRGPVATV LVREGTLHKG
DIVLCGFEYG RVRAMRNELG QEVLEAGPSI PVEILGLSGV PAAGDEVTVV RDEKKAREVA
LYRQGKFREV KLARQQKSKL ENMFANMTEG EVHEVNIVLK ADVQGSVEAI SDSLLKLSTD
EVKVKIIGSG VGGITETDAT LAAASNAILV GFNVRADASA RKVIDAESLD LRYYSVIYHL
IDEVKAAMSG MLSPELKQQI IGLAEVRDVF KSPKFGAIAG CMVTEGTIKR HNPIRVLRDN
VVIYEGELES LRRFKDDVNE VRNGMECGIG VKNYNDVRVG DMIEVFEIIE IQRTID
