IF2_SYMTH
ID IF2_SYMTH Reviewed; 1044 AA.
AC Q67P86;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=STH1522;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD40507.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67P86; -.
DR SMR; Q67P86; -.
DR STRING; 292459.STH1522; -.
DR EnsemblBacteria; BAD40507; BAD40507; STH1522.
DR KEGG; sth:STH1522; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR Proteomes; UP000000417; 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; 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; PF04760; IF2_N; 2.
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..1044
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228252"
FT DOMAIN 546..714
FT /note="tr-type G"
FT REGION 55..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..562
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 580..584
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 601..604
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 655..658
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 691..693
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 102..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 601..605
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 655..658
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1044 AA; 110586 MW; A60569269F5717D4 CRC64;
MEPRLRVFEL ARELGVDSKR VLEVLQSLNV DVKNHMSTID QKTAEKVTDA VRRTEAQEGQ
GAGKSAAKSA KPAAQPKPTR EANPAKTSLL EDFFGSGTRP QRPLSEKRER RPLTERRPLA
ERRPLAERPL VDRPVTERPL AERPAAELRP GAAKAAAPAR PAAEAQPVAE RRAPAEAAQA
AQAERRPAEK AQPAAAAKAA PPEKAGAAPV PGAVAEQKQA ATPAAAEQKP AGKAEQTAGA
AQAKPARAEA GTGASSRPAS AAPAAQGEKR PAAAAERREE PQAEAPQTSG PSRPVPAGPG
QPARPAGSGI GVPVKPAAGG KSGLGLPTRP GEKAADGARG GGSGIGLPVK PAAGQGTAAR
AGGLGLPQKP KAGAPRPGGG LGAPQRPGRR GAPLAIPKLD PKVAEQAKAG EGKPRYGQSG
DKRRADLYDR REHPSSQPSE EKLFGQRPKR KASAQERRVL KPITVTGPMS VKDLAHEMGV
TAAEVIKTLL TGFGIMATIN QELDVDTCVL VASEFGVEAT VEQKEDIIEV YDRVEDPDEP
AELKKPRHPV VTIMGHVDHG KTSLLDAIRQ AKVAAGEAGG ITQHIGAYEV ELNGRKITFL
DTPGHEAFTA MRARGANVTD IAVLVVAADD SVMPQTVESI NHAKAANVPI LVAINKIDKP
EANPQRVMQD LTQYGLVPEE WGGDTIMVPV SAKQKTNLDL LLENILVLAE VSDLKANPDK
PAAGTILEAA LDKARGPVAT VLVQAGTLNT GDVFVAGTSW GRVRAMFDHR GRKLKSAGPS
TPVRVLGFDS VPQAGDVFRV TPDEKTARAI AEKRIAKAQA ERLAQKAISL DDFMNQVAQG
EIKDLNVIVK ADVQGSVEAI RGQLEKLRNE EVKVKVIHAG VGAISESDVM LAVASKAIII
GFNVRPDDRA SRAADEHGID VRTYSVIYDI VDDIEAAMKG MLKPKIEEVI LGKAEVRETF
KVPKVGMAAG CMVIQGKVTR NARYRLIRDG VVVWDGEINA LRRFKDEVRE VSEGYECGIT
LQNFHDFKRG DILEAYELQE IKAG
