IF2_SODGM
ID IF2_SODGM Reviewed; 894 AA.
AC Q2NW23;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SG0377;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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; AP008232; BAE73652.1; -; Genomic_DNA.
DR RefSeq; WP_011410240.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NW23; -.
DR SMR; Q2NW23; -.
DR STRING; 343509.SG0377; -.
DR PRIDE; Q2NW23; -.
DR EnsemblBacteria; BAE73652; BAE73652; SG0377.
DR KEGG; sgl:SG0377; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; SGLO343509:SGP1_RS03550-MON; -.
DR Proteomes; UP000001932; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..894
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008341"
FT DOMAIN 393..562
FT /note="tr-type G"
FT REGION 52..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..409
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 427..431
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 448..451
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 538..540
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 448..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 894 AA; 97841 MW; FA9106A10FE18635 CRC64;
MTDVTVKSLA AEIQTPVDRL VQQFADAGID KTAVDSVTQQ EKETLLAHLN RDRGAAPNKL
TLQRKTRSTL NIPSTGGKSK SVQIEVRKKR TYVQRDPQAQ EQAEAEEQAR REAEELAQHQ
VQRDAEEKAK RAAEDKAKRE AAEQAKRVAA ESDKLTNQQT NTMTKSPQAT EKARREAEAA
ELRRKAEEET RRKVEEKARQ VAEEARRMAE ERGGNWDNAP EPAEEDTTDY HVNTSHHARE
AEDENDRKVE GDRRSRTRGG KATKQKKTSR LSESKADREE ARAVGRGGKG KRRPSTLTQG
FNKPAQAVNR DVVIGETITV AELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA
EEMGHKVILR RENELEESVM SDRDTGSSAA AESRAPVVTI MGHVDHGKTS LLDYIRSTKV
AAGEAGGITQ HIGAYHVETD NGMITFLDTP GHAAFTAMRA RGAQATDIVV LVVAADDGVM
PQTIEAIQHA KAAKVPVVVA VNKIDKPEAD PDRVKNELTQ YGVIPEEWGG ESQFVHVSAK
SGAGIDELLD AILLQAEVLE LKAIRNGMAS GVVIESFLDK GRGPVATVLV REGTLNRGDI
VLCGFEYGRV RAMRDEVGRD VASAGPSIPV EILGLSGVPA AGDEATVVRD EKKAREVALY
RQGKFREVKL ARQQKSKLEN MFANMTEGEV SELNIVLKSD VQGSAEAISD ALEKLSNDEV
KVKIVGSGVG GITETDATLA AASNAILLGF NVRADASARR VIEAENLDLR YYSVIYDLID
EVKQAMSGML APEYKQEIIG LAEVRNVFRS PKFGAIAGCM VTEGVVKRHN KIRVLRENVV
IYEGELESLR RFKDDVNEVR NGMECGIGVK NYNDVRSGDV IEVFETIEIQ RTIA
