IF2_SHESH
ID IF2_SHESH Reviewed; 896 AA.
AC A8FYS0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ssed_3389;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
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., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-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; CP000821; ABV37993.1; -; Genomic_DNA.
DR RefSeq; WP_012143723.1; NC_009831.1.
DR AlphaFoldDB; A8FYS0; -.
DR SMR; A8FYS0; -.
DR STRING; 425104.Ssed_3389; -.
DR PRIDE; A8FYS0; -.
DR EnsemblBacteria; ABV37993; ABV37993; Ssed_3389.
DR KEGG; sse:Ssed_3389; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002015; 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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075621"
FT DOMAIN 394..563
FT /note="tr-type G"
FT REGION 53..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..410
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 428..432
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 449..452
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 539..541
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 449..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 96155 MW; 1D5D45055005C8A5 CRC64;
MADTTVEKLA SEVGKSADRL VEQFSEAGIK KSKADTVSES EKQQLLEFLK KQHGGESAPT
KMTLQRKSVS TLSVGSGSAS KDVKVEVRKK RTFVKRDPAA DAEAEAAAKA EAEVKAAEEA
ASKAKADAEA KAKAEAKAKA DAEAKEKAKA SAAEKAKPVA VTAEEKAAQD EADKLQAAKD
TAAKAKADEE AKAAAEIARK LAEENSARWA EEEKQRKESE KTGDHHVTTS TEARAAEDTA
DANAEKRGRR PRKATPAPAA APANTGKGKR RGGKDNRRDS RNARGGRNAR NNRSVAPESM
DHAFTKPVAA VKTDVSIGET VSVSELASKM SIKATEIIKQ MMKMGSMVTI NQVLDQETAQ
LVAEEMGHKV VLTRENELEH QVLADRDANI QAESRAPVVT IMGHVDHGKT SLLDYIRRAK
VASGEAGGIT QHIGAYHVET DNGMITFLDT PGHAAFTAMR ARGAQATDIV ILVVAADDGV
MPQTIEAIQH AKAGGVPLIV AVNKIDKPEA DPERVKSELS QHGVMSEDWG GNNMFVHVSA
KSGEGIDELL EGILLEAEVL ELKAIKEGMA AGVVVESKLD KGRGPVATVL VQEGTLKQGD
IVLCGLEYGK VRAMRDENGR AIKEAGPSIP VEILGLSGVP SAGDEATVVR DERKAREVAL
YRQGKFRDVK LARQQKSKLE NMFANMVEGE VQELNIILKA DVQGSLEAIA DSLNKLSTDE
VKVNIIARGV GGLTETDASL AAASNAIMIG FNIRADAQAR KVIDAESVDL RYYSVIYHLI
DEVRNAMSGL LAPEFKQVIL GLAEVRDVFK SPKIGAIAGC MVTEGTIKRS APIRVLRENV
VIYEGELESL RRFKDDVADV RNGMECGIGV KNYNDVRVGD QIEVFETIEI ARSLEE
