ID   IF2_PEDPA               Reviewed;         918 AA.
AC   Q03FS3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PEPE_0890;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
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; CP000422; ABJ67949.1; -; Genomic_DNA.
DR   RefSeq; WP_011673322.1; NC_008525.1.
DR   AlphaFoldDB; Q03FS3; -.
DR   SMR; Q03FS3; -.
DR   STRING; 278197.PEPE_0890; -.
DR   PRIDE; Q03FS3; -.
DR   EnsemblBacteria; ABJ67949; ABJ67949; PEPE_0890.
DR   GeneID; 33062166; -.
DR   KEGG; ppe:PEPE_0890; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 103279at2; -.
DR   Proteomes; UP000000773; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..918
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008294"
FT   DOMAIN          419..588
FT                   /note="tr-type G"
FT   REGION          39..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..435
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          453..457
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          474..477
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          528..531
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          564..566
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        39..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         428..435
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         474..478
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         528..531
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   918 AA;  101974 MW;  6A84FB1D6DBC196B CRC64;
     MGKKRIYELA KEINVSSKDI IEKAQADGLD VKNHMSTLDD ASEKHLRNAF KKNTTTTKPE
     EKRTPKFRSS KTGKTVVKKS DHPAADGTKG IQRLKSSNNE STTRNNNNNK NGNQNRNNTN
     GRPNNNQNRP NNNRNQNNNR NGNRPNQPKR DEKQDRIRAS VAEAARMAAQ ANREIANEKP
     QANRQRTNSA KPGEQRREGR NNQNRPNNNN RNGNNVNRTN NNNRPNNNNR NNENRPSRPN
     NTNQTTNNRP ANNTTRPAAP AATTANNSGE KKQDRFSGRN NNSRGGNRFG NNQNRPFNKE
     NRKNKKRNRK AKRDGRMKET TNKVVTVRKE RPLPDVLEYS EGINVAEIAK KIHREPAEII
     KKLFMMGVMV NQNQSLDNDT VELLAADYGI EAQQKVEVDI SDIDKIFEDE EKNTTNLVSR
     PPVVTIMGHV DHGKTTLLDK LRHSHITEGE AGGITQGIGA YQLKHDDKLI TFLDTPGHAA
     FTEMRARGAD VTDITILVVA ADDGVMPQTI EAINHAKAAN VPIIVAVNKI DKQGANPNHV
     MEQLTEYGLI PESWGGDTIF VEISAKLGQN IDELLDMILL QAEVLELKAN PDQNAAGSVI
     EAQLDPGKGS IATILVQQGT MHVGDPIVIG NTFGRIRTMV NEHGRRVKEA TPSTPVEITG
     LNGVPEAGDR FVVFDDEKSA RAAGEERAKR AQMEERKRSN HVTLDNLFDS LKEGEMKKVD
     IIIKADVQGS VEALADSLQK IEVEGVRVNI IHKAVGAINE SDVTLAAASN AIIIGFNVRP
     TAQAKQMADS EDVDIRLHRV IYNAIDEVES AMKGMLEPVY EEEIIGQVDI RETYKVSRVG
     TIAGGFVTEG FITRDSGVRL IRDGVVIYEG KLGSLKRFKD DVKEVKRGFE LGLTVENYND
     IKIGDVIEAY RMKEVPVE