IF2_BORPA
ID IF2_BORPA Reviewed; 969 AA.
AC Q7W9A5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BPP1862;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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; BX640428; CAE37163.1; -; Genomic_DNA.
DR RefSeq; WP_010928245.1; NC_002928.3.
DR AlphaFoldDB; Q7W9A5; -.
DR SMR; Q7W9A5; -.
DR EnsemblBacteria; CAE37163; CAE37163; BPP1862.
DR KEGG; bpa:BPP1862; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR Proteomes; UP000001421; 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.
FT CHAIN 1..969
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137175"
FT DOMAIN 470..637
FT /note="tr-type G"
FT REGION 96..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..486
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 504..508
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 525..528
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 579..582
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 615..617
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 120..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 525..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 579..582
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 969 AA; 103545 MW; 9F816DA9A456524A CRC64;
MSSNTVAQFA TELKMPANVL LEQLRAAGVD LKSVDDAVTD SDKAKLLESL RRAHGATEGK
KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPA EPVRAEPAVE TAAKPVEPPV
AEAPAEPVAA PAAEPQPEQP AQAEAQPEPT PAAQAEPEPQ PEPQPEAAPA QAVAEPVEPA
KNVSVTETEA EQARPEPVVH AQTELTSQTP APVAQPSAPA ESPKSAKAEP AAAPKTTAKP
GEIRRAAAPA APDRAREEAR RAAEAEAAAL REMLSRPRKV LRAPEPEPQA GALSGTLHKP
AGKPATTAAP KKDAKPGAPG AKKTIKTAEV SSTWSDDSAR KKPADNKPAV TTRDGWRAGG
KGGRGGRNSR NQHQDRRHEQ VQQEFIAREI HVPETISVAD LAHKMSVKAA EVIKQLMKLG
QMVTINQVLD QETAMIVVQE FGHTAIAAKL DDPEAFLDET AAVTEAEAEP RAPVVTVMGH
VDHGKTSLLD YIRRAKVASG EAGGITQHIG AYHVETGRGV VTFLDTPGHE AFTAMRARGA
KATDIVILVV AADDGVMPQT REAIHHAKAG GVPLVVAVNK IDKPEANPER VKQELVAEEV
VPEEYGGDVP FVPVSAKTGA GIDDLLENVL LQAEILELKA PIEVPAKGLV IEARLDKGRG
PVATILVQSG TLKRGDVVLA GASFGRVRAM LDENGKQIQT AGPSIPVEIQ GLTEVPAAGD
ELMVLSDERK AREIALFRQG KFRDVKLARQ QAAKLESMFD NLGEGTQTLA LIVKTDVQGS
QEALVSSLTK LSTDEVRVQV VHAAVGGISE SDVNLAIASN AVVIGFNVRA EQSAKKLAET
NGIDLRYYNI IYDAVDEVKA AMSGMLAPEK REEVIGLVEV REVYTISRIG TVAGCMVLDG
VVRRDSQVRL LRNNVVQWTG HLDSLRRFKD DVKEVKSGFD CGLTLRGNND LQLGDQLEVF
EIKEIARTL
