IF2_BORPE
ID IF2_BORPE Reviewed; 997 AA.
AC Q7VYR2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BP1247;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX640414; CAE41543.1; -; Genomic_DNA.
DR RefSeq; NP_880019.1; NC_002929.2.
DR RefSeq; WP_010930271.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYR2; -.
DR SMR; Q7VYR2; -.
DR STRING; 257313.BP1247; -.
DR PRIDE; Q7VYR2; -.
DR KEGG; bpe:BP1247; -.
DR PATRIC; fig|257313.5.peg.1343; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002676; 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..997
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137176"
FT DOMAIN 498..665
FT /note="tr-type G"
FT REGION 101..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..514
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 532..536
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 553..556
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 607..610
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 643..645
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 148..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 507..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 553..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 607..610
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 997 AA; 106159 MW; C8DC28C3170BFFD5 CRC64;
MSSNTVAQFA TELKMPANVL LEQLRAAGVD LKSVDDAVTD SDKAKLLESL RRAHGATEGK
KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPA ELAAEQAAAR AEEAAAEAVP
AEAAPAPAEP VRAEPAVETA AKPVEPPVAE APAEPVAAPA AEPQPEQPAQ AEAQPEPTPA
AQAEPEPQPE PQPEAAPAQA VAEPVEPAKN VSVTETEAEQ ARPEPVVHAQ TELTSQTPTP
VAQPSAPAES PKSVKAEPAA APKTTAKPGE IRRAAAPAAP DRAREEARRA AEAEAAALRE
MLSRPRKVLR APEPEPQAGA LSGTLHKPAG KPATTAAPKK DAKPGAPGAK KTIKTAEVSS
TWSDDSARKK PADNKPAVAT RDGWRAGGKG GRGGRNSRNQ HQDRRHEQVQ QEFIAREIHV
PETISVADLA HKMSVKAAEV IKQLMKLGQM VTINQVLDQE TAMIVVQEFG HTAIAAKLDD
PEAFLDETAA VTEAEAEPRA PVVTVMGHVD HGKTSLLDYI RRAKVASGEA GGITQHIGAY
HVETGRGVVT FLDTPGHEAF TAMRARGAKA TDIVILVVAA DDGVMPQTRE AIHHAKAGGV
PLVVAVNKID KPEANPERVK QELVAEEVVP EEYGGDVPFV PVSAKTGAGI DDLLENVLLQ
AEILELKAPI EAPAKGLVIE ARLDKGRGPV ATILVQSGTL KRGDVVLAGA SFGRVRAMLD
ENGKQIQTAG PSIPVEIQGL TEVPAAGDEL MVLSDERKAR EIALFRQGKF RDVKLARQQA
ANLESMFDNL GEGTQTLALI VKTDVQGSQE ALVSSLTKLS TDEVRVQVVH AAVGGISESD
VNLAIASNAV VIGFNVRAEQ SAKKLAETNG IDLRYYNIIY DAVDEVKAAM SGMLAPEKRE
EVIGLVEVRE VYTISRIGTV AGCMVLDGVV RRDSQVRLLR NNVVQWTGHL DSLRRFKDDV
KEVKSGFDCG LTLRGNNDLQ LGDQLEVFEI KEIARTL
