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IF2_SHESR
ID   IF2_SHESR               Reviewed;         885 AA.
AC   Q0HXR5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Shewmr7_1091;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) 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; CP000444; ABI42090.1; -; Genomic_DNA.
DR   RefSeq; WP_011621817.1; NC_008322.1.
DR   AlphaFoldDB; Q0HXR5; -.
DR   SMR; Q0HXR5; -.
DR   EnsemblBacteria; ABI42090; ABI42090; Shewmr7_1091.
DR   KEGG; shm:Shewmr7_1091; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
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   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..885
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008336"
FT   DOMAIN          385..554
FT                   /note="tr-type G"
FT   REGION          135..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..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        184..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;  96188 MW;  0A0A8414698CC8E1 CRC64;
     MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGHTDNVSEA EKQQLLDYLK KQHGGDNAPT
     KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDAN DAVLKAEEEA KAKAEAEAKA
     KAEAEAKAKA EAEVKAKAEA EAKAKAEAEA KAKAKAAAEV KVIKELSPEA EAARVEAERL
     KAVQAEATKR KQDEEAAKAA EKARLLAEEN SKRWAEEERQ RLEAERYSDH HITTSKVARA
     AEDSSDMDEE KRGRRARNKN TAKSKRGGKD ARDGREKHMR NRSTAPESMA HGFNKPVAAV
     NRDVRIGETV TVAELAHLMA VKATEIIKQM MKMGSMVTIN QVLDQETAQL VAEEMGHKVV
     LIRENELEQQ VLSERDEEGV VKLEPRAPVV TIMGHVDHGK TSLLDYIRRA KVAAGEAGGI
     TQHIGAYHVE TDNGMITFLD TPGHAAFTAM RARGAKATDI VVLVVAADDG VMPQTIEAIQ
     HAKAGNVPLI VAVNKMDKPE ADIDRVKSEL AQHGVMSEDW GGDNMFAFVS AKTGAGVDDL
     LEGILLQAEV LELKAVRDGM AAGVVIESQL DKGRGPVATI LVQEGTLRQG DIVLCGLEYG
     KIRAMKDENG RSITEAGPSI PVEILGLSGV PSAGDEATVV RDERKAREVA LYRQGKFRDV
     KLARQQKSKL ENMFANMTEG EVKELNIVLK ADVQGSLEAI TDSLMGLSTD EVKVNIIARG
     VGALTETDAT LAAASNAIMV GFNVRADAQA RKTIESESVD LRYYSVIYNL IDEVKAAMTG
     MLSPEFKQQI IGLAEVRDVF KSPKLGAIAG CMVTEGTIKR SAPIRVLRDN VVIFEGELES
     LRRFKDDVNE VRNGMECGIG VKNYNDVRVG DQIEVFETVE VARTL
 
 
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