IF2_BORA1
ID IF2_BORA1 Reviewed; 1034 AA.
AC Q2KXY7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BAV2394;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(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; AM167904; CAJ50004.1; -; Genomic_DNA.
DR RefSeq; WP_012418055.1; NC_010645.1.
DR AlphaFoldDB; Q2KXY7; -.
DR SMR; Q2KXY7; -.
DR STRING; 360910.BAV2394; -.
DR PRIDE; Q2KXY7; -.
DR EnsemblBacteria; CAJ50004; CAJ50004; BAV2394.
DR GeneID; 41394232; -.
DR KEGG; bav:BAV2394; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001977; 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; 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..1034
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008204"
FT DOMAIN 535..702
FT /note="tr-type G"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..551
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 569..573
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 590..593
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 644..647
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 680..682
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 257..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 590..594
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 644..647
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1034 AA; 109420 MW; E444ECF276F29D9A CRC64;
MSSNTVAQFA TELKMPANVL LEQLRAAGVD LKSVDDSVTD SDKAKLLDSL RRAHGATDGK
KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPA ELAAEAAAEA KAAAEQAAAE
AVDMQPESVE AQAPAPQSVE ALAQAPVEAV KPVEAEAPKI ETPPVETPAV EAVEAAAPKI
EASEAPAEPV QTQTAQAVEE TPAPAETPEP VPAVKAEAEP QSAQPAASRE QSTAQPVEPE
AKKESVAAPK TQEAGPESVV HAQTDLNSKT PAPVAKSETA PSAPKAAQGR PQVAEAARPP
VVNDRAREDA RRAAEAEAAA LREMLNRPRK VLRAPEPEPA GTNNAALSGT LHKPAGKKDA
AAAPAAAPKK EGGNKPAAAG AGGKKVIKTA EVSSTWNDDA SRKKPADKAA APGGNSRDGW
RSGGKGGGKN SRNGRNQHQD RRNESAAQEF IAREIHVPET ISVADLAHKM SVKAAEVIKQ
LMKLGQMVTI NQVLDQETAM IVVEELGHVA IAAKLDDPEA FLDETPGVSE AEALPRAPVV
TVMGHVDHGK TSLLDYIRRA KVAAGEAGGI TQHIGAYHVE TDRGSVTFLD TPGHEAFTAM
RARGAKATDI VILVVAADDG VMPQTREAIH HAKAAGVPLV VAVNKIDKPE ANPDRVKQEL
VAEQVVPEEY GGDVPFVPVS AKTGAGIDDL LENVLLQAEI LELTAPVEAA AKGIVIEARL
DKGRGPVATI LVQSGTLKRG DVVLAGASFG RVRAMLDENG KQVQSAGPSI PVEIQGLTEV
PAAGDELISL SDERRAREIA LFRQGKFRDV KLARQQAAKL ESMFDNMGEG TQTLPLIVKT
DVQGSQEALV AALTKLSTDE VRVQVVHAAV GGISESDVNL AIASNAVVIG FNVRADQSAK
KLADNNGIDL RYYNIIYDAV DEVKAAMSGM LAPEKREEII GLVEVREVYT ISRIGTVAGC
MVLDGLVRRD SQVRLLRNNV VTWTGQLDSL RRFKDDVKEV KSGFDCGLTL RGNNDLQMGD
QLEVFEIKEI ARTL
