IF2_PARP8
ID IF2_PARP8 Reviewed; 965 AA.
AC B2JKT4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bphy_1729;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC70911.1; -; Genomic_DNA.
DR RefSeq; WP_012401121.1; NZ_CADFGH010000004.1.
DR AlphaFoldDB; B2JKT4; -.
DR SMR; B2JKT4; -.
DR STRING; 391038.Bphy_1729; -.
DR PRIDE; B2JKT4; -.
DR EnsemblBacteria; ACC70911; ACC70911; Bphy_1729.
DR KEGG; bph:Bphy_1729; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001192; 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; Reference proteome.
FT CHAIN 1..965
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093765"
FT DOMAIN 465..634
FT /note="tr-type G"
FT REGION 94..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..481
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 499..503
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 520..523
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 574..577
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 610..612
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 118..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 520..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 574..577
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 965 AA; 103849 MW; 5702FFBEB6EE4529 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RRSHGSNDAD
KRKITLTKRH TSEIKQSDAT GKARTIQVEV RKKRTFVRRD EAAEQAAEAT GNGQEAAEDL
ELQRREEEAR HEAELLEKQA QELKARQEQL AREEAERQAR EQAAEAERRR AEEEAAKKRA
AAVAEAAAAA REQAEQERAS QDEERAAAER AAQREAAKKA EDAAREQAEK ARLEQEEIAK
RRAKAEAEAR AIREMMNTPR KAQVKAPEPP PKPAEAPKPA EAKGTLHKPA RPAGETSARP
AAKKPAPAAA AQPAATTQPA GPGGDKKKAG GKGGWQDDAA KRRGIKTRGD TSGGVDRGWR
GGPKGRGKHQ ESTTFQAPTE PIVREVHVPE TITVADLAHK MSVKASEVIK VMMKLGQMVT
INQMLDQETA MIVVEELGHH AVAAKLDDPE AMLVEGEASD APQLPRPPVV TVMGHVDHGK
TSLLDYIRRA KVAAGEAGGI TQHIGAYHVE TPRGVITFLD TPGHEAFTAM RARGAKATDI
VILVVAADDG VMPQTKEAIS HAKAGGVPLV VAINKIDKPE ANPERVKQEL VAEGVVPEEY
GGDSPFVPVS AKTGAGIDDL LENVLLQAEV LELKAPVEAP AKGLVIEAKL DKGKGPVATI
LVQSGTLNRG DVVLAGSAYG RVRAMLDETG KPTKAAGPSI PVEIQGLSEV PAAGEEVIVM
PDDRKAREVA LFRQGKFRDV KLAKQQAAKL ENMLEQMGEG EVQYLPLIVK ADVQGSQEAL
VQSLLKLSND EVRVQIVHSA VGGISESDVN LATASKAVII GFNTRADAQA RKLAESNGID
IRYYNIIYDA VDEVKAAMSG MLAPEKREVV TGMVEVRQVF KVPKVGAVAG CMVTDGVVKR
TSSVRVLRNN VVIHTGELDS LKRFKDDVKE VRQGFECGMS VKNFNDIMEG DQFEVFEVTE
VARTL
