IF2_PAEAT
ID IF2_PAEAT Reviewed; 958 AA.
AC A1R516;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AAur_1561;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(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; CP000474; ABM09969.1; -; Genomic_DNA.
DR RefSeq; WP_011774273.1; NC_008711.1.
DR AlphaFoldDB; A1R516; -.
DR SMR; A1R516; -.
DR STRING; 290340.AAur_1561; -.
DR PRIDE; A1R516; -.
DR EnsemblBacteria; ABM09969; ABM09969; AAur_1561.
DR KEGG; aau:AAur_1561; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000637; 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 PRINTS; PR00315; ELONGATNFCT.
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..958
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335456"
FT DOMAIN 450..621
FT /note="tr-type G"
FT REGION 67..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..466
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 484..488
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 509..512
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 563..566
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 599..601
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 71..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 459..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 509..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 563..566
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 958 AA; 98838 MW; C114B0F0E7A3A947 CRC64;
MAKVRVHELA KELGITSKDA VTKLQELGEF VRSASSTIEA PVVKKLRDAY PGAGAAKAAA
PAAAPKAPAA SRPAAPAPGP AAPKAPAPAP AAPAPAAPAA AAPAAAAPAA PAPAAPAAPA
ASTPVSAKPG ARPAPKAETP APARQGGQAP RPGGPRPGNN PFATSQGMPR GRGGDGDRPP
RPGNNPFAPS QGMPRGERRN DGERPGGPRP AAGAGGPRPA AGTGGPRPGA PRPGAPRPGA
PRPAGGPGAG NRPTPGMMPN RTERPAPGGA GRPGGAGRPG GGPGRPGGAP GAGTGGGAPA
GGGFGKGGRG RGGTQGAFGK GGAGRGKQRK SKRAKRQELE QMSAPSLGGV SVPRGDGETI
IRLRRGSSIT DFAEKIDANP ASLVTVLFHL GEMATATQSL DEDTFGLLGA ELGYKLQVVS
PEDEERELLD QFDINIQDEL DAEGDDVLEA RAPVVTVMGH VDHGKTRLLD AIRNSNVVAG
EHGGITQHIG AYQISHVHEG KARDITFIDT PGHEAFTAMR ARGAKVTDIA ILVVAADDGV
MPQTVEALNH AQAANVPIVV AVNKIDKEGA NPDKVKGQLT EYGLVPEEYG GDTMFVEVSA
RQNLNIDELI DAVLLTADAA LDLRANPDKD ARGIAIEANL DKGRGAVATV LVQSGTLAVG
DTIVAGTAHG RVRAMFDENG EALDVALPSR PVQVLGLSNV PRAGDTFLVT PDERTARQIA
EKREAADRNA ALAKRRKRIS LEDFDQAVAE GKIDTLNLIL KGDVSGAVEA LEDALLKIDV
GDDDVQLRVI HRGVGAITQN DVNLATVDNA IIIGFNVKPA ERVAELADRE GVDMRFYSVI
YAAIDDIEMA LKGMLKPEYE EVQLGTAEVR EVFRSSKFGN IAGSIVRTGI IRRNSKARVS
RDGKVIGDNL TVETLKRFKD DATEVRTDFE CGIGLGSFND INEGDIIETF EMREKPRS
