IF2_STRP4
ID IF2_STRP4 Reviewed; 930 AA.
AC B5E266;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SPG_0502;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) 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; CP001015; ACF56844.1; -; Genomic_DNA.
DR RefSeq; WP_000039200.1; NC_011072.1.
DR AlphaFoldDB; B5E266; -.
DR SMR; B5E266; -.
DR KEGG; spx:SPG_0502; -.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
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.
FT CHAIN 1..930
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093831"
FT DOMAIN 432..599
FT /note="tr-type G"
FT REGION 50..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..448
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 466..470
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 487..490
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 541..544
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 577..579
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 487..491
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 541..544
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 930 AA; 102936 MW; 7ACDD2A30455807B CRC64;
MSKKRLYEIA KELGKESKEV VARAKELGLD VKSHSSSVEE AVAAKIAASF KPAAAPKVEA
KPAAPKVSAE KKAEKSEPAK PAVAKEEAKP AEPVAPKTEK VAAKPQSRNF KAEREARAKE
QAERRKQNKG NNRDQQQNGN RQKNDGRNGG KQGQSNRDNR RFNDQAKKEQ GQQKRRNERR
QQEDKRSNQV APRIDFKARA AALKAEQNAE YARSSEERFK QYQAAKEALA QANKRKEPEE
IFEEAAKLAE QAQQVQAVVE VVPEKKEPAV DTRRKKQARP DKNRDDYDHE EDGPRKQQKN
RSSQNQVRNQ KNSNWNNNKK NKKGNNKNNR NQTPKPVTER KFHELPTEFE YTDGMTVAEI
AKRIKREPAE IVKKLFMMGV MATQNQSLDG ETIELLMVDY GIEAKQKVEV DNADIERFFV
EDGYLNEDEL VERPPVVTIM GHVDHGKTTL LDTLRNSRVA TGEAGGITQH IGAYQIVENG
KKITFLDTPG HAAFTSMRAR GASVTDITIL VVAADDGVMP QTIEAINHSK AANVPIIVAI
NKIDKPGANP ERVIGELAEH GVMSTAWGGD SEFVEISAKF NQNIEELLET VLLVAEIQEL
KADPTVRAIG TVIEARLDKG KGAVATLLVQ QGTLNVQDPI VVGNTFGRVR AMTNDLGRRV
KVAGPSTPVS ITGLNEAPMA GDHFAVYEDE KSARAAGEER AKRALMKQRQ ATQRVSLENL
FDTLKAGELK SVNVIIKADV QGSVEALSAS LQKIDVEGVK VTIVHSAVGA INESDVTLAE
ASNAFIVGFN VRPTPQARQQ AEADDVEIRL HSIIYKVIEE MEEAMKGMLD PEFEEKVIGE
AVIRETFKVS KVGTIGGFMV INGKVARDSK VRVIRDGVVI YDGELASLKH YKDDVKEVTN
GREGGLMIDG YNDIKMDDVI EAYVMEEIKR
