IF2_SHEB5
ID IF2_SHEB5 Reviewed; 880 AA.
AC A3D7K6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sbal_3239;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
RG US DOE Joint Genome Institute;
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 Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-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; CP000563; ABN62719.1; -; Genomic_DNA.
DR RefSeq; WP_006082716.1; NC_009052.1.
DR AlphaFoldDB; A3D7K6; -.
DR SMR; A3D7K6; -.
DR STRING; 325240.Sbal_3239; -.
DR EnsemblBacteria; ABN62719; ABN62719; Sbal_3239.
DR GeneID; 11774928; -.
DR KEGG; sbl:Sbal_3239; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001557; 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..880
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008328"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 180..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 880 AA; 95543 MW; FBF6000CC76DD082 CRC64;
MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGQADNVTEA EKQQLLDYLK KQHGGENAPT
KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDAN EATLKAEEEA KVEAEALAKA
KAEAEAAAAV KAKAEADAKA KADAEAKAKA KAAAEVKVVK DMSPEAEAAR LEAERLKAAQ
EAATKRKQDE EAAKAAETAR LLAEEHSKRW AEEERQRLEA EKNGDHHITT SKVARAAEDT
SDLDEEKRGR RARNKSNAKK RGGKDARDGR EKHMRNRSTA PESMAHGFNK PVAAVSRDVR
IGETVTVSEL AHLMAVKATE IIKQMMKMGS MVTINQVLDQ ETAQMVAEEM GHKVVLIREN
ELEHQVLKDR DDEDGIKQES RAPVVTIMGH VDHGKTSLLD YIRRAKVAAG EAGGITQHIG
AYHVETENGM ITFLDTPGHA AFTAMRARGA KATDIVVLVV AADDGVMPQT IEAIQHAKAG
NVPLIVAVNK MDKPEADIDR VKSELSQHGV MSEDWGGDNM FAFVSAKTGE GVDELLEGIL
LQAEVLELKA VRDGMAAGVV IESQLDKGRG PVATILVQEG TLRQGDIVLC GLEYGKIRAM
KDENGRSITE AGPSIPVEIL GLSGVPSAGD EATVVRDERK AREVALYRQG KFRDVKLARQ
QKSKLENMFA NMTEGEVKEL NIVLKADVQG SLEAITDSLT GLSTDEVKVN IIARGVGALT
ETDATLAAAS NAILVGFNVR ADAQARKTID SESVDLRYYS VIYNLIDEVR AAMTGMLSPE
FKQQIIGLAE VRDVFKSPKL GAIAGCMVTE GTIKRSAPIR VLRDNVVIYE GELESLRRFK
DDVAEVRNGM ECGIGVKNYN DVRVGDQIEV FETVEIARTL
