IF2_SHEFN
ID IF2_SHEFN Reviewed; 881 AA.
AC Q086H2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, 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}; OrderedLocusNames=Sfri_0990;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-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; CP000447; ABI70843.1; -; Genomic_DNA.
DR RefSeq; WP_011636464.1; NC_008345.1.
DR AlphaFoldDB; Q086H2; -.
DR SMR; Q086H2; -.
DR STRING; 318167.Sfri_0990; -.
DR PRIDE; Q086H2; -.
DR EnsemblBacteria; ABI70843; ABI70843; Sfri_0990.
DR KEGG; sfr:Sfri_0990; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000684; 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..881
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008331"
FT DOMAIN 381..550
FT /note="tr-type G"
FT REGION 142..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..397
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 415..419
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 526..528
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 142..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 881 AA; 95938 MW; 9939FEB6E3746D43 CRC64;
MADTSVEKLA AEVGKSVDRL IEQFSQAGMN KKQLDTVSEK EKQQLLDYLK KQHGADSVPT
KMTLQRKTVS TLSVASTGGQ SKDVKVEVRK KRTFVKRDDA ELAKQAELET QAKAKAEAEA
QAKVEAEAKA AAEAKATADA KKKAEAEAKL KSEKVKSEPK VTKVADPETA AAKVEADRLK
ATQEAVLTQK QKDEAAKAAE TARQLAEVNS KRWAEEERQR LDAEKNGDHH ITTSKVARAA
EDSSDADDEK RGRRARNKNA NKKRGGKDAR DGREKHMRNR STAPESMAHG FNKPAAAVSR
DVRIGETVTV SELAHLMAIK ATVIIKQMMK MGTMVTINQV LDQETAQMVA EELGHKVVLI
RENELEHQVL KDRDDNIQLE SRAPVVTIMG HVDHGKTSLL DYIRRAKVAA GEAGGITQHI
GAYHVETENG MITFLDTPGH AAFTSMRARG AKATDIVILV VAADDGVMPQ TIEAIQHAKA
GNVPLIVAVN KMDKPDADPE RVKSELSQHG IMSDDWGGDN MFVHVSAKTG MGVDELLEGI
LLQSEVLELK AVRDGMAAGV VIESQLDKGR GPVATILVQE GTLRQGDIVL CGLEYGKIRA
MKDENGHAIT EAGPSIPVEI LGLSGVPSAG DEATVVRDER KAREVALYRQ GKFRDVKLAR
QQKSKLENMF ANMEEGEVQE LNIVLKADVQ GSLEAICESL AKLSTDEVKV NIIARGVGAL
TETDATLAAA SNAILVGFNV RADAQARKTI DSESVDLRYY SIIYNLIDEV RAAMTGMLAP
EFRQEIIGLA EVRDVFKSPK IGAIAGCMVT EGIVKRSAPI RVLRDNVVIF EGELESLRRF
KDDAPEVRNG MECGIGVKNY NDVRVGDQIE VFETVEIART L
