IF2_OENOB
ID IF2_OENOB Reviewed; 829 AA.
AC Q04GN0;
DT 20-MAY-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=OEOE_0433;
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000411; ABJ56392.1; -; Genomic_DNA.
DR RefSeq; WP_002818231.1; NC_008528.1.
DR AlphaFoldDB; Q04GN0; -.
DR SMR; Q04GN0; -.
DR STRING; 203123.OEOE_0433; -.
DR EnsemblBacteria; ABJ56392; ABJ56392; OEOE_0433.
DR KEGG; ooe:OEOE_0433; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 84734at2; -.
DR Proteomes; UP000000774; 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; 1.
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..829
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335494"
FT DOMAIN 329..498
FT /note="tr-type G"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..345
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 363..367
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 384..387
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 474..476
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 37..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 338..345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 384..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 829 AA; 90524 MW; 6BA7F76912224C20 CRC64;
MTEEEKKRRP LVHHIRKQSA SKSELPASQR RHAAGLSSRA QGERHGEKTP TNNQDSRQRR
RVSFDSNTGR PAPKDHKPIH AGSASAPAGS SLNQPRKTTS QRQRTNSRTS KTTVEPLRRA
HPHNPLPNQH PVTNQRNNRR NNNRTAGGQS SNNRNNNNHK TNASQNGTGR FGGALASGNN
SARNNTRRRN QTTTAPGTHF VSGPARGIRR KSGPKGSKKA QRIAAAAVSK NRQNERKEQP
LPKVLEYRLG MNVQDIAKII HRDVTEILKK LFLLGVVVNQ NQSLDADTIE LLAADYNIEA
KQKEEVDVSD IDRFFDKTDN DIDQSKLVSR APIVTIMGHV DHGKTTLLDY LRHTHVTEGE
AGGITQRIGA YQARLHDRLI TFLDTPGHEA FTEMRARGAN VTDITILVVA ADDGIMPQTI
EAIHHAQAAK TPIIVAINKI DIPGVDPNNV INELMKYDLV PEEYGGSTIE VPISAKTGQN
VDKLLEMILL QADMMDLKSD PTAKSRGSVI EARLDKGRGA VATLLIQQGT LKTGDPIVVG
NTFGRVRTMN DASHKKLDSA LPATPVEITG LNEVPQAGDH FVVMDSEKDA REAGESRAKK
AMEEERNNGA VVTLDTLFST MAKRDMKTVS LIVKADVQGS VEALSASLKK IKVEGVRVDI
LHAAVGAINE SDINLAEASG AIIIGFNVRP VGQAKTDAEQ KHVDVRLYNV IYDAINEVEA
AMKGQLEPVY KEKTLGTVSV RELFHFSKIG TIAGGLVTDG IITSDSKVRL VRDGVVVYDG
QLGSLKHGKD DVKEVKKGFE LGLTIANYND EKVGDVIEAY TMEEVKANA
