IF2_STRTD
ID IF2_STRTD Reviewed; 943 AA.
AC Q03M88;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=STER_0383;
OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=322159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-491 / LMD-9;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000419; ABJ65684.1; -; Genomic_DNA.
DR RefSeq; WP_011680757.1; NC_008532.1.
DR AlphaFoldDB; Q03M88; -.
DR SMR; Q03M88; -.
DR KEGG; ste:STER_0383; -.
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..943
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008357"
FT DOMAIN 445..614
FT /note="tr-type G"
FT REGION 29..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..461
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 479..483
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 590..592
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 29..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 554..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 943 AA; 103824 MW; E66470CAF95BBC1B CRC64;
MSKKRLYEIA KEVGVESKVI VAKAQELGLS VKSHSSSVEE ADANRITSSL KAGTAKDESK
PAPKATPTPK EEKVEPKVDK ASVAKSAPAK ETSKAEVKEA SVALKKPKSR NFKAEREARA
KAEAERRKNG GGRDNRNRNQ QGNDQGKRHN NDRRNQKGNG QGDHNKGNRD NSTNHDRNFQ
GKLRNDQNQN NRRDNARNNQ AGPRIDLKAR AAALKAEQNA EYSRQSETRF REEKAAEQRR
AKEQEKARKE KQQAEVAVQK AAAETKPAPK PAPVAPQSAP TAQVQDTRRK KVRPNKSRDN
HRVNEDGPKQ TRNNKWNNQN QVRNQRNSNW NKNKNKKGKN NRGNSAPKLV TERKFHELPK
EFEYTEGMTV AEIAKRIKRE PAEIVKKLFM MGVMATQNQS LDGDTIELLM VDYGIEATKK
EEVDNADIER FFVDEDYLNK DAMVERAPVV TIMGHVDHGK TTLLDTLRNS RVATGEAGGI
TQHIGAYQIE EGGKKITFLD TPGHAAFTSM RARGASVTDI TVLIVAADDG VMPQTIEAIN
HSKAAGVPII VAINKIDKPD ANPERVIGEL AEHGVISTAW GGDSEFVEIS AKFGQNIEEL
LETILLVAEV EELKADPTVR AIGTVIEARL DKGKGAVATL LVQQGTLNVQ DPIVVGNTFG
RVRAMTNDLG RRIKTAGPSA PVSITGLNEA PMAGDHFAVY EDEKAARAAG EERAKRALMK
QRQQTHRVSL DNLFDTLKAG EMKTVNVIIK ADVQGSVEAL AASLLKIDVE GVRVNVVHSA
VGAINESDIT LAEASDAVVI GFNVRPTPQA RQQAETDEVE IRLHSIIYKV IEEIEDAMKG
MLDPEFEEKI IGEAVIRETF KVSKVGTIGG FMVTNGKITR DSSARVIRDG VVIFDGKLAS
LKHYKDDVKE VGNAQEGGLT IENYNDIKVD DVIEAYIMEE IKR
