IF2_BURM9
ID IF2_BURM9 Reviewed; 975 AA.
AC A2S2L1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=BMA10229_A0175;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN03072.1; -; Genomic_DNA.
DR RefSeq; WP_004197388.1; NC_008836.1.
DR AlphaFoldDB; A2S2L1; -.
DR SMR; A2S2L1; -.
DR EnsemblBacteria; ABN03072; ABN03072; BMA10229_A0175.
DR GeneID; 56595459; -.
DR KEGG; bml:BMA10229_A0175; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002283; Chromosome I.
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..975
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008212"
FT DOMAIN 475..644
FT /note="tr-type G"
FT REGION 48..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..491
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 509..513
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 530..533
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 584..587
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 620..622
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 48..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 484..491
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 530..534
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 584..587
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 975 AA; 104751 MW; 447642044BA93AA7 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
KRKITLTRRH TSEIKQADAT GKARTIQVEV RKKRTFVKRD DVSETGADQA QAQTDEQAEA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
AAAQAEAAQQ AAAAREQAQR AQSEPAEQSA QDEARAAAER AAQREAAKKA EDAAREAADK
ARAEQEEIRK RREAAEAEAR AIREMMNTPR RAQVKAVEPP KPAEPPAAKA AEAKGTLHKP
AKPAGEAAAA RPAAKKPASG APAPAAAPAG DRTKKPGTGK SGWQDDAAKR RGIKTRGDSS
GGVDRGWRGG PKGRGKHQDS ASSFQAPTEP IVREVHVPET ISVADLAHKM SIKASEVIKV
MMKMGQMVTI NQVLDQETAM IVVEELGHRA LAAKLDDPEA LLVEGEIGSD AEQLPRPPVV
TVMGHVDHGK TSLLDYIRRA KVAAGEAGGI TQHIGAYHVE TPRGVVTFLD TPGHEAFTAM
RARGAKATDI VILVVAADDG VMPQTKEAIS HAKAGGVPIV VAINKIDKPE ANPDRVKQEL
VAEGVVPEEY GGDSPFVPVS AKTGAGIDDL LENVLLQAEV LELKAPVESP AKGIVIEAKL
DKGKGPVATV LVQSGTLSRG DVVLAGTAYG RVRAMLDENG KPTKEAGPSI PVEIQGLSEV
PGAGDEVIVL PDERKAREIA LFRQGKFRDV KLAKQQAAKL ESMLEQMGEG EVQNLPLIIK
ADVQGSQEAL VQSLLKLSTD EVRVQIVHSA VGGISESDVN LATASKAVII GFNTRADAQA
RKLAEANGID IRYYNIIYDA VDEVKAAMSG MLAPEKREVV TGMVEVRQVF KVPKVGTVAG
CMVTDGVVKR SSSVRVLRNN VVIFTGELDS LKRFKDDVKE VKQGFECGMS LKNFNDIVEG
DQFEVFEVTE VARTL
