IF2_ROSDO
ID IF2_ROSDO Reviewed; 824 AA.
AC Q16D38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RD1_0386;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG30105.1; -; Genomic_DNA.
DR RefSeq; WP_011566727.1; NZ_FOOO01000001.1.
DR AlphaFoldDB; Q16D38; -.
DR SMR; Q16D38; -.
DR STRING; 375451.RD1_0386; -.
DR PRIDE; Q16D38; -.
DR EnsemblBacteria; ABG30105; ABG30105; RD1_0386.
DR KEGG; rde:RD1_0386; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000007029; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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.
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..824
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008325"
FT DOMAIN 321..489
FT /note="tr-type G"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..337
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 355..359
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 377..380
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 431..434
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 467..469
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 377..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 431..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 824 AA; 88506 MW; B0D0FB2CF399ADE3 CRC64;
MSDTDGKKTL GLRGGAPRPG NVKQSFSHGR TKNVVVETKR KRVVVPKAGA TTSAGGKAPI
GDPSRRPAGI SDAEMERRLK AVKAAKAREA EEEAARIAEE KARAEERERR RAEQEERERA
EREREESLKA KAEEDKRRKD EAEAAAKAAA APAAEPVVQR PAAKAAPEPA PRKQQDRDRD
NKRGGKGNDD SRRSGKLTLN QALAGGEGGR QRSMAAMKRK QERARQKAMG GQVEREKVVR
DVQVPEAIVV SELANRMSEK VGEVVKALMN NGMMVTQNQA IDADTAELIV QEFGHRIVRV
SDADVEDVIK EVEDDEADLK TRPPVVTIMG HVDHGKTSLL DAIRKAKVVA GEAGGITQHI
GAYQVKTDSG QLLSFLDTPG HAAFTSMRSR GAQVTDIVVL VVAADDAVMP QTIEAINHAK
AAEVPMIVAI NKIDRPAADP TKVRTDLLQH EVIVEQMSGD VQDVEVSAIT GQGLDDLLEA
IALQAEILEL KANPNRAAQG AVIEAQLDVG RGPVATVLVQ NGTLRQGDIF VVGEQYGKVR
ALINDQGERV KEAGPSVPVE VLGLNGTPEA GDVLNVTSTE AQAREIASYR ANAAKDKRAA
AGAATTLEQL MANAKADEDV SELPILVKAD VQGSAEAIVQ AMEKIGNDEV RVRVLHSGVG
AITETDVGLA EASGAPIMGF NVRANASARN TANQKGVELR YYSIIYDLVD DVKAAASGLL
SAEIRENFIG YATIKEVFKV TGVGKVAGCL VTEGVARRSA GVRLLRDNVV IHEGTLKTLK
RFKDEVAEVQ SGQECGMAFE NYDDIRADDV IEIFEREEIT RTLT
