IF2_SHEPA
ID IF2_SHEPA Reviewed; 896 AA.
AC A8H740;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Spea_3060;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) 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. {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; CP000851; ABV88377.1; -; Genomic_DNA.
DR RefSeq; WP_012156281.1; NC_009901.1.
DR AlphaFoldDB; A8H740; -.
DR SMR; A8H740; -.
DR STRING; 398579.Spea_3060; -.
DR PRIDE; A8H740; -.
DR EnsemblBacteria; ABV88377; ABV88377; Spea_3060.
DR KEGG; spl:Spea_3060; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002608; 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; Reference proteome.
FT CHAIN 1..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075620"
FT DOMAIN 396..563
FT /note="tr-type G"
FT REGION 117..303
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 117..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..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:0000255|HAMAP-Rule:MF_00100"
FT BINDING 451..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 505..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 96151 MW; DCA69DB71B639C16 CRC64;
MADTTVDKLA TEVGKSTERL VEQFSQAGIK KSASDTVSET EKQQLLDFLK KQHGGDAAPT
KMTLQRKSVS TLSVAGSGGQ SKDVKVEVRK KRTFVKRDEA AEAELAAAAK AEEAKAAEAE
AKAKAEAEAK AKVDAEAKVK AKAEAEAKAK AKVQTEKPAA ETAEDKAAKA EEAKLLAAQD
AVAKAKANEE ASAAADEARR LAEENEKRWA EEEKARKEAE KSVDHHVTTS TEARAAEDTA
DANAEKRGRR PRKPSANAGN NANANAGAGK PGGKGKRGKD NRRDNRNSRN SRNTRSVAPE
SMDHAFTKPA AVVKAEVSIG ETVSVAELAS KMSIKATEII KQMMKMGSMV TINQVLDQET
AQLVAEEMGH KVILTRENEL EHQVLADRNG DVKVEPRAPV VTIMGHVDHG KTSLLDYIRR
AKVASGEAGG ITQHIGAYHV ETENGMITFL DTPGHAAFTA MRARGAKATD IVILVVAADD
GVMPQTIEAI QHAKAGGVPL IVAVNKIDKP EADPDRVKSE LSQHGVMSED WGGNNMFVHV
SAKDGTGIDE LLEGILLEAE VLELQAVREG MAAGVVVESK LDKGRGPVAT VLVQEGTLKQ
GDIVLCGLEY GKVRAMRDEN GKAITEAGPS IPVEILGLSG VPSAGDEATV VRDERKAREV
ALYRQGKFRD VKLARQQKSK LENMFANMVE GEVQELNLVL KADVQGSLEA IADSLNSLST
DEVKVNIIAR GVGGLTETDA TLAAASNAIM VGFNVRADAQ ARKVVDSESV DLRYYSIIYQ
LIDEVRDAMS GMLAPEFKQE IIGLAEVRDV FKSPKIGAIA GCMVTEGTIK RSAPIRVLRD
NIVIYEGELE SLRRFKDDVS DVRNGMECGI GVKNYNDVRV GDQIEVFETV EIARTL
