IF2_PARPJ
ID IF2_PARPJ Reviewed; 986 AA.
AC B2T381;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bphyt_1632;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(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}.
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DR EMBL; CP001052; ACD16042.1; -; Genomic_DNA.
DR RefSeq; WP_012432653.1; NC_010681.1.
DR AlphaFoldDB; B2T381; -.
DR SMR; B2T381; -.
DR STRING; 398527.Bphyt_1632; -.
DR EnsemblBacteria; ACD16042; ACD16042; Bphyt_1632.
DR KEGG; bpy:Bphyt_1632; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001739; Chromosome 1.
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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR SUPFAM; SSF46955; SSF46955; 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.
FT CHAIN 1..986
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093766"
FT DOMAIN 486..655
FT /note="tr-type G"
FT REGION 95..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..502
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 520..524
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 541..544
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 595..598
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 631..633
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 95..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 541..545
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 595..598
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 986 AA; 105634 MW; 704049E1165EA258 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVT KASEDDSLSE TDKARLLDHL RKSHGSTDAD
KRKITLTKRH TSEIKQSDAT GKARTIQVEV RKKRTFVRRD ETSAENGDAS NHVAEADVDD
LELQRREEEA RHEAELLEKQ AQELKARQEQ LEREEAERQA REAAAEAERR RAEEEAAKKR
AAAEAAAREQ AQAAKPAQAA QPAAAKAEPV AAKAAEPAVA KQSEQDDERA AAERAAQREA
AKKAEDAARQ AAEKARAEQE QIAKRRAAAE AEARAIREMM NTPRKAQVKA PEPAPKPAEP
AKAAEAKGTL HKPARPAGEA PSRPAAKKPA AAAPAATTTP SAGDKKKPGG GKGGWQDDAA
KRRGIKTRGD TSGGVDRGWR GGPKGRGKHQ DQNTTFQAPT EPIVREVHVP ETITVADLAH
KMAVKASEVI KSMMKLGQMV TINQMLDQET AMIIVEELGH HAVAAKLDDP EAMLVEGEIS
DAESLPRPPV VTVMGHVDHG KTSLLDYIRR AKVAAGEAGG ITQHIGAYHV ETPRGVITFL
DTPGHEAFTA MRARGAKATD IVILVVAADD GVMPQTKEAI AHAKAGGVPL VVAINKIDKP
DANPDRVKQE LVAEGVVPEE YGGDSPFVSV SAKTGAGIDD LLENVLLQAE VLELKAPVEA
PAKGLVIEAK LDKGKGPVAT ILVQSGTLNR GDVVLAGSAY GRVRAMLDET GKPTKSAGPS
IPVEIQGLSE VPQAGEEVIV MPDDRKAREV ALFRQGKFRD VKLAKQQAAK LENMLEQMGE
GEVAYMPLIV KADVQGSQEA LVQSLLKLST DEVRVQIVHG AVGGISESDV NLATASKAVI
IGFNTRADAQ ARKLAEANGV DIRYYNIIYD AVDEVKAAMS GMLAPEKREI VTGTVEVRQV
FKVPKIGAVA GCMVTDGFVK RSSSVRVLRN NVVIFTGELD SLKRFKDDVK EVRQGFECGM
SIKNFNDIVE GDQFEVFEIT EVARTL
