IF2_SHEON
ID IF2_SHEON Reviewed; 885 AA.
AC Q8EHL5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SO_1204;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54274.1; -; Genomic_DNA.
DR RefSeq; NP_716829.1; NC_004347.2.
DR RefSeq; WP_011071434.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EHL5; -.
DR SMR; Q8EHL5; -.
DR STRING; 211586.SO_1204; -.
DR PaxDb; Q8EHL5; -.
DR KEGG; son:SO_1204; -.
DR PATRIC; fig|211586.12.peg.1156; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR PhylomeDB; Q8EHL5; -.
DR BioCyc; SONE211586:G1GMP-1116-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..885
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137246"
FT DOMAIN 385..554
FT /note="tr-type G"
FT REGION 123..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..401
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 419..423
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 440..443
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 494..497
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 530..532
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 123..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 440..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 494..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 885 AA; 96113 MW; 055A1E38CF6B24EE CRC64;
MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGQADNVSEA EKQQLLDYLK KQHGGDNAPT
KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDVS DAVLKAEEEA KAKAEAEAKA
KAETEAKAKA EAEAKAKVEA EAKAKAEAEA KAKAKAAAEV KVTKDTSPEA EAARIEAERL
KAAQEAATKR KQAEEAAKAA EKARLLAEEN SKRWAEEERQ RLEAERYSDH HITTSKVARA
AEDSSDMDEE KRGRRARNKN TAKTKRGGKD ARDGREKHMR NRSTAPESMA HGFNKPVAAV
NRDVRIGETV TVAELAHLMA VKATEIIKQM MKMGSMVTIN QVLDQETAQL VAEEMGHKVV
LIRENELEQQ VLSERDEEGG VKLEPRAPVV TIMGHVDHGK TSLLDYIRRA KVAAGEAGGI
TQHIGAYHVE TENGMITFLD TPGHAAFTAM RARGAKATDI VVLVVAADDG VMPQTIEAIQ
HAKAGNVPLI VAVNKMDKPE ADIDRVKSEL SQHGVMSEDW GGDNMFAFVS AKTGAGVDDL
LEGILLQAEV LELKAVRDGM AAGVVIESQL DKGRGPVATI LVQEGTLRQG DIVLCGLEYG
KIRAMKDENG RSITEAGPSI PVEILGLSGV PSAGDEATVV RDERKAREVA LYRQGKFRDV
KLARQQKSKL ENMFANMTEG EVKELNIVLK ADVQGSLEAI TDSLMGLSTD EVKVNIIARG
VGALTETDAT LAAASNAIMV GFNVRADAQA RKTIENESVD LRYYSVIYNL IDEVKAAMTG
MLSPEFKQQI IGLAEVRDVF KSPKLGAIAG CMVTEGTIKR SAPIRVLRDN VVIFEGELES
LRRFKDDVNE VRNGMECGIG VKNYNDVRVG DQIEVFETVE VARTL
