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IF2_SHEB2
ID   IF2_SHEB2               Reviewed;         880 AA.
AC   B8E6N2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Sbal223_1128;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-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; CP001252; ACK45643.1; -; Genomic_DNA.
DR   RefSeq; WP_006082716.1; NC_011663.1.
DR   AlphaFoldDB; B8E6N2; -.
DR   SMR; B8E6N2; -.
DR   EnsemblBacteria; ACK45643; ACK45643; Sbal223_1128.
DR   GeneID; 11774928; -.
DR   KEGG; sbp:Sbal223_1128; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002507; 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_1000190632"
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
 
 
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