IF2_STRGC
ID IF2_STRGC Reviewed; 953 AA.
AC A8AVQ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SGO_0546;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09252.1; -; Genomic_DNA.
DR RefSeq; WP_012000047.1; NC_009785.1.
DR AlphaFoldDB; A8AVQ2; -.
DR SMR; A8AVQ2; -.
DR STRING; 467705.SGO_0546; -.
DR EnsemblBacteria; ABV09252; ABV09252; SGO_0546.
DR KEGG; sgo:SGO_0546; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001131; 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..953
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075625"
FT DOMAIN 455..622
FT /note="tr-type G"
FT REGION 53..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..471
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 489..493
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 510..513
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 564..567
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 600..602
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 953 AA; 105035 MW; 7A25CB7B8670949F CRC64;
MSKKRLYEIA KELGKESKEI VQRAKELGLD VKSHSSSVEA ATADKIVASF ASAKKAVAGT
SEAKAKPSTE PIKTEATPSK PAKDKTEQAT NKPSPSPASS PKPVEEASAK APASKQEQAQ
GTAAPKVTRP QSRNFKAERE ARAKEQAERR KQQGQQRPQG NRNDRNDRRN NQNDRNDRNS
QNRNDRRNRQ EQGNQHRNQG QSQYNQQRQS FNQGPKIDFK ARAAALKAEQ NAEYARSSEE
RFKQAKANKE ALREQNKRKE QAKLEDLFVE VESPKPTAKA PATPAPTAQD PAVDTRRKKQ
ARPDKERDNF DHEEDGPRKQ QKNRSSQNQV RNQKNSNWNN NKKTKKGKNN RNNNATPKPV
TERKFHELPT EFEYTDGMTV AEIAKRIKRE PAEIVKKLFM MGVMATQNQS LDGDTIELLM
VDYGIEAKKK VEVDAADIER FFVEEGYINE DALEERPPVV TIMGHVDHGK TTLLDTLRNS
RVATGEAGGI TQHIGAYQIV EGGKKITFLD TPGHAAFTSM RARGASVTDI TILVVAADDG
VMPQTIEAIN HSKAANVPII VAINKIDKPG ANPERVIGEL AEHGVMSTAW GGDSEFVEIS
AKFNQNIDEL LETVLLVAEI QELKADPTVR AIGTVIEARL DKGKGAVATL LVQQGTLNVQ
DPIVVGNTFG RVRAMTNDLG RRVKVAGPST PVSITGLNET PMAGDHFAVY EDEKAARAAG
EERAKRALLK QRQATHRVSL ENLFDTLKAG EVKSVNVIIK ADVQGSVEAL AASLQKIEVE
GVKVTIVHSA VGAINESDVT LAEASNAVII GFNVRPTPQA RQQAESDSVE IRLHSIIYKV
IEEVEDAMKG MLDPEYQEKI IGEALIRETF KVSKVGTIGG FMVISGKVTR DSKVRVIRDG
VVIYDGQLAS LKHFKDDVKE VTNGREGGLM IEGYNDIQVD DTIEAYIMEE IKK
