IF2_SHESW
ID IF2_SHESW Reviewed; 880 AA.
AC A1RGX5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Sputw3181_1070;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000503; ABM23920.1; -; Genomic_DNA.
DR RefSeq; WP_011788443.1; NC_008750.1.
DR AlphaFoldDB; A1RGX5; -.
DR SMR; A1RGX5; -.
DR PRIDE; A1RGX5; -.
DR GeneID; 45043323; -.
DR KEGG; shw:Sputw3181_1070; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002597; 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_1000008337"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 143..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 143..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; 95516 MW; 1944E05E354A7126 CRC64;
MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGQADNVSEA EKQQLLDYLK KQHGADSAPT
KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDVN DTVLKAEEEA KAEAEALAKA
KAEAEAAQAA KAKAEAEAKA KAEAEAKAKA KAAAEVKVTK ESSPEVEAAR LEAERLKAAQ
EAATKRKQDE EAAKAAEKAR LLAEENSKRW AEEERQRLEA ERNGDHHITT SKVARAAEDT
SDLDEEKRGR RARNKSNAKK RGGKDARDGR EKHMRNRSTA PESMAHGFNK PVAAVSRDVR
IGETVTVSEL AHLMAVKATE IIKQMMKMGS MVTINQVLDQ ETAQLVAEEM GHKVVLIREN
ELEHQVLQDR DDEDGIKLES RAPVVTIMGH VDHGKTSLLD YIRRAKVAAG EAGGITQHIG
AYHVETENGM ITFLDTPGHA AFTAMRARGA KATDIVVLVV AADDGVMPQT IEAIQHAKAG
NVPLIVAVNK MDKPEADIDR VKSELSQHGV MSEDWGGDNM FAFVSAKTGE GVDDLLEGIL
LQAEVLELKA VRDGMAAGVV IESQLDKGRG PVATILVQEG TLRQGDIVLC GLEYGKIRAM
KDENGRSITE AGPSIPVEIL GLSGVPSAGD EATVVRDERK AREVALYRQG KFRDVKLARQ
QKSKLENMFA NMTDGEVKEL NIVLKADVQG SLEAITDSLT GLSTDEVKVN IIARGVGALT
ETDATLAAAS NAIMVGFNVR ADAQARKVIE SESVDLRYYS VIYNLIDEVK AAMTGMLSPE
FKQQIIGLAE VRDVFKSPKL GAIAGCMVTE GTIKRSAPIR VLRDNVVIFE GELESLRRFK
DDVAEVRNGM ECGIGVKNYN DVRVGDQIEV FETVEVARTL
