IF2_SHEDO
ID IF2_SHEDO Reviewed; 884 AA.
AC Q12QI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sden_1007;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
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 Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-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; CP000302; ABE54295.1; -; Genomic_DNA.
DR RefSeq; WP_011495459.1; NC_007954.1.
DR AlphaFoldDB; Q12QI1; -.
DR SMR; Q12QI1; -.
DR STRING; 318161.Sden_1007; -.
DR PRIDE; Q12QI1; -.
DR EnsemblBacteria; ABE54295; ABE54295; Sden_1007.
DR KEGG; sdn:Sden_1007; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001982; 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; Reference proteome.
FT CHAIN 1..884
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008330"
FT DOMAIN 384..553
FT /note="tr-type G"
FT REGION 110..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..400
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 418..422
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 439..442
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 529..531
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 110..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 439..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 884 AA; 95784 MW; F8CE26EFCA958B61 CRC64;
MADTSVQKLA AEVGKSVERL IEQFSEAGLK KGQADTVSET EKQQLLDYLK KQHGADKAPT
KMTLQRKTVS TLSVPAGGGQ SKDVKVEVRK KRTFVKRDDS ELVDQAELEA KAKAEADAKA
AAEAKQKADA EAQAKAAAEA KAKAEANKAK EKAPQAPAPK PKAELKAETP EAAAARAEAE
RIKATQEAVL TKKQKEEAAQ AAEEAKKLAE VNSKRWAEEE RLRLEAEKNG DHHVTTSKVA
RAAEDSSDMD DEKRGRRARN KPTNKKRGGK DARDGREKHM RNRSTAPQSM AHGFNKPVAA
VSRDVRIGET VSVAELAHLM AVKATEIIKQ MMKMGSMVTI NQILDQETAQ MVAEEMGHKV
VLLRENELEE QVLGDRDDNV KLETRAPVVT IMGHVDHGKT SLLDYIRRAK VAAGEAGGIT
QHIGAYHVET DNGMITFLDT PGHAAFTSMR ARGAKATDIV ILVVAADDGV MPQTIEAIQH
AKAGNVPLIV AVNKMDKPDA DPERVKSELS QHGVMSDDWG GDNMFVHLSA KTGEGVDELL
EGILLQSEVL ELKAVREGMA AGVVIESQLD KGRGPVATVL VQSGTLRQGD IVLCGLMYGK
IRAMKDENGN AITEAGPSIP VEILGLSGVP SAGDEATVVR DERKAREVAL YRQGKFRDVK
LARQQKSKLE NMFANMEEGE VQELNIVLKA DVQGSLEAIC DSLTGLSTAE VKVNIIARGV
GALTETDATL AAASNAIMVG FNVRADAQAR KTIEAESVDL RYYSIIYNLI DEVRAAMTGM
LAPEFKQQII GLAEVRDVFK SPKIGAIAGC MVTEGIVKRS APIRVLRDNV VIYEGELESL
RRFKDDATEV RNGMECGIGV KNYNDVRVGD QIEVFETIEV ARTL
