IF2_SHELP
ID IF2_SHELP Reviewed; 885 AA.
AC A3QGU5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Shew_2827;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
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., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-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; CP000606; ABO24693.1; -; Genomic_DNA.
DR RefSeq; WP_011866624.1; NC_009092.1.
DR AlphaFoldDB; A3QGU5; -.
DR SMR; A3QGU5; -.
DR STRING; 323850.Shew_2827; -.
DR EnsemblBacteria; ABO24693; ABO24693; Shew_2827.
DR KEGG; slo:Shew_2827; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001558; 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..885
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008332"
FT DOMAIN 385..554
FT /note="tr-type G"
FT REGION 51..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..295
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 58..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..280
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; 95159 MW; 20A37967D577522D CRC64;
MADTTVAKLA EEVGKSADRL VEQFSEAGIK KSKTDTVSED EKQKLLEFLK KQHGGDSAPT
KMTLQRKSIS TLSVSGSGGQ SKDIKVEVRK KRTFVKRDVA AEAEAEAKAK AEAEAKAAAE
AEAKAKADAE AKAKAEAEAA AKAKAKAEAE AKAKKAAEGK PAAEETAEEK AAKVEEARLL
AAKEAAAKAK ADEEAKAAAE EARRLAEENE KRWAEEERLR KESENSADHH VTTSTEARAA
EDSADRDAER RGRRARKPAG GKKEPIGKKR GGKEARGGRN NRNQRNAPES MDHGFNKPAA
AVTRDVTIGE TVTVAELAQK MAVKATEIIK QMMKMGSMVT INQVLDQETA QLVAEEMGHK
VVLTRENELE HQVLADRDGN VKVEPRAPVV TIMGHVDHGK TSLLDYIRRA KVASGEAGGI
TQHIGAYHVE TDNGMITFLD TPGHAAFTAM RARGAKATDI VVLVVAADDG VMPQTIEAIQ
HAKAGGVPLI VAVNKIDKPE ADPDRVKSEL SQHGVMSEDW GGNNMFVHVS AKSGEGIDEL
LEGILLEAEV LELKAVREGM AAGVVVESKL DKGRGPVATI LVQEGTLKQG DIVLCGLEYG
KVRAMKDENG KSITEAGPSI PVEILGLSGV PSAGDEATVV RDERKAREVA LYRQGKFRDV
KLARQQKSKL ENMFANMTEG EVQELNIVLK ADVQGSLEAI SDSLNKLSTD EVKVNIIASG
VGGLTETDAT LAAASNAIMV GFNVRADAQA RKTIESESVD LRYYSVIYHL IDEVKAAMGG
MLAPEFKQEI IGLAEVRDVF KSPKIGAIAG CMVTEGTIKR SAPIRVLRDN VVIFEGELES
LRRFKDDVNE VRNGMECGIG VKNYNDVKVG DQIEVFETVE IARTL
