IF2_SHEHH
ID IF2_SHEHH Reviewed; 893 AA.
AC B0TQA2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Shal_3147;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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; CP000931; ABZ77694.1; -; Genomic_DNA.
DR RefSeq; WP_012278218.1; NC_010334.1.
DR AlphaFoldDB; B0TQA2; -.
DR SMR; B0TQA2; -.
DR STRING; 458817.Shal_3147; -.
DR PRIDE; B0TQA2; -.
DR EnsemblBacteria; ABZ77694; ABZ77694; Shal_3147.
DR KEGG; shl:Shal_3147; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001317; 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..893
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075619"
FT DOMAIN 393..562
FT /note="tr-type G"
FT REGION 135..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..409
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 427..431
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 448..451
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 538..540
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 201..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 448..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 893 AA; 95663 MW; BD7F0ADDF621E7BF CRC64;
MADTTVDKLA TEVGKSTDRL VEQFSQAGIK KSANDTVSES EKQQLLDFLK KQHGGDAAPT
KMTLQRKSVS TLSVAGSGGQ SKDVKVEVRK KRTFVKRDEA AEAELAAAAK AEEAKAAEVA
KTAAEAKAKL DAEAKAKAKA DAEAKAKAKV LTEKPVQESA EDKAAKAEEA KLLAAQDAAA
KSKADEDVAA AAEVARRLAE ENEKRWAEEE KARKEAEKTV DHHVTTSTEA RAAEDTADAN
AEKRGRRPRK PSANAGNNAN ANAGAGKPGG KGKRGKDNRR DSRNSRNSRN NRSVAPESMD
HAFTKPAAVV KADVSIGETV SVSELASKMS IKATEIIKQM MKMGSMVTIN QVLDQETAQL
VAEEMGHKVV LTRENELEHQ VLADRNGDVL AESRAPVVTI MGHVDHGKTS LLDYIRRAKV
ASGEAGGITQ HIGAYHVETE NGMITFLDTP GHAAFTAMRA RGAKATDIVI LVVAADDGVM
PQTIEAIQHA KAGGVPLIVA VNKMDKPEAD PDRVKSELSQ HGVMSEDWGG NNMFVNVSAK
TGAGIDELLE GILLEAEVLE LKAIKEGMAA GVVVESKLDK GRGPVATVLV QEGTLKQGDI
VLCGLEYGKV RAMRDENGKA ITEAGPSIPV EILGLSGVPS AGDEATVVRD ERKAREVALY
RQGKFRDVKL ARQQKSKLEN MFANMTEGEV EELNIVLKAD VQGSLEAICD SLNALSTAEV
KVNIIARGVG GLTETDATLA AASNAIMVGF NVRADAQARK VVESESVDLR YYSIIYQLID
EVRDAMSGLL APEFKQEIIG LAEVRDVFKS PKIGAIAGCM VTEGTIKRSA PIRVLRDNIV
IYEGELESLR RFKDDVSDVR NGMECGIGVK NYNDVRVGDQ IEVFETVEIA RTL
