IF2_OLEA2
ID IF2_OLEA2 Reviewed; 984 AA.
AC Q30WJ0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dde_3162;
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB39956.1; -; Genomic_DNA.
DR RefSeq; WP_011368911.1; NC_007519.1.
DR AlphaFoldDB; Q30WJ0; -.
DR SMR; Q30WJ0; -.
DR STRING; 207559.Dde_3162; -.
DR EnsemblBacteria; ABB39956; ABB39956; Dde_3162.
DR KEGG; dde:Dde_3162; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002710; 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..984
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228192"
FT DOMAIN 482..651
FT /note="tr-type G"
FT REGION 32..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..498
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 516..520
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 537..540
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 591..594
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 627..629
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 47..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491..498
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 537..541
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 591..594
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 984 AA; 105452 MW; B87E128CF7667D85 CRC64;
MSETKIKIKD LATELNIAPK EVLAAAKKLD IPAKNATSTL TTEEARKVRG QVQEASGDAR
RKDGASDVII RRRRKGSGAK PAAREEAAPA ETEAQASPAQ PEAKAAAPAA EAEEAPAAKP
APAKARKAEA RTEAPRARII RPATPQAEEK AEPAPETAAP AQPAPEAQSA APEKVEAHDA
GAPVQQAETT ESAPAEPAAE KAPAEKRRYE VSMEPEKDSV QADTEADGDA DGGRKKKKKK
KREETAGPQV RVISRPDPAA VQAQAAAAAQ AREERAERPD RGPRPAGARP AGPRPGGPRQ
GDSRPGDGRP APRSGAPRPG GARPAAGFGQ PAQAENSSPF ADGQSKKKRQ KGRRTVEFGD
KGAGGKKMRE DVGGNWNRGK KGKRKPETKP VSTQPQRAAK RKIKVDEAIR VSDFAHQMGV
KAPEIIKILM SLGIMATINQ SLDIDTATVV AAEFGYEVEK VGFSEDEFLL PKEVDADELL
LPRPPVVTIM GHVDHGKTSL LDAIRKSSVT TGEAGGITQH IGAYHVSTKR GDIVFLDTPG
HEAFTAMRAR GAQVTDLVIL VVAADDGVME QTREAISHAK AAGVPIVVAV NKIDKEGANR
DRVMRELAEQ DLVPEEWGGD TIFSYVSAKT REGLDDLLEM LALQAEVLEL KANPDKPARG
RIVEAKLDKG RGAVGTVLIQ EGTLKHGDAF VCGVFSGRVR AMFNDQGKKA KQAGPSIPVE
VQGFEGVPVA GEEFICVKDE KVARRIAEQR AIKQRERDLA RESKVTLETF LARRKTDAET
QTLNLVLKAD VQGSVGAITD ALRKMQTEKV KVDIIHSGAG AITESDILLA SASDAIIIGF
NVRPTAKVKD VAEQEKVEIR FYDIIYKLSE EIKSAMAGLL APVVREQYLG QAEVRETFSV
PKVGTVAGCH VADGKIIRNT KVRLLRDGVV IYTGRINSLK RFKDDVKEVA KGFECGMGLE
NYNDIKIGDI IEAFEEVEEA ATLD
