IF2_BORPD
ID IF2_BORPD Reviewed; 991 AA.
AC A9ITX6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bpet3133;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP43475.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ITX6; -.
DR SMR; A9ITX6; -.
DR STRING; 94624.Bpet3133; -.
DR PRIDE; A9ITX6; -.
DR EnsemblBacteria; CAP43475; CAP43475; Bpet3133.
DR KEGG; bpt:Bpet3133; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; RDVMMAG; -.
DR Proteomes; UP000001225; 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..991
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093760"
FT DOMAIN 492..659
FT /note="tr-type G"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..508
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 526..530
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 601..604
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 637..639
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 165..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 547..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 601..604
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 991 AA; 104344 MW; 90A833E9BB4D7211 CRC64;
MSSNTVAQFA TELKMPANVL LEQLRSAGVD LNSVDDAVTD SDKAKLLDSL RRAHGATEGK
KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPS EIALEQARAD AAASDAAPAE
PAPAAAEPSA SAPVTAPVNA PAADAPQAPA TAAPDTAAPA AETPSQPPAV EPQPAPVAQA
EPEPQPEPVA KPAEAPAEPA APAAVEAHAE REAEQAPPEP AVQAEIETAP APAAESAQAA
RPEPVTPKAE PAPAASKPAR AEGRRGAPVP VAAPAVDSAG REEARRAAEA EAAALREMLN
RPRKVLRAPE PEAGALSGTL HKPAGKAAAP GAKKDAKPGA GGSKKTIKTA EVASTWSDDA
SRKKPADTKS AAPSRDGWRA GGKGGKGGRN SRNQQAERRH EPAPQEFIAR EVHVPETISV
ADLAHKMSVK AAEVIKQLMK LGQMVTINQV LDQETAMIVV EELGHVAIAA KLDDPEAFLD
ETPVASEAEA LPRAPVVTVM GHVDHGKTSL LDYIRRAKVA SGEAGGITQH IGAYHVETAR
GVVTFLDTPG HEAFTAMRAR GAKATDIVIL VVAADDGVMP QTREAIHHAK AGGVPLVVAV
NKIDKPEANP ERVKQELVAE EVVPEEYGGD VPFVPVSAKT GAGIDDLLEN VLLQAEILEL
TAPVEAPAKG LVIEARLDKG RGPVATILVQ SGTLKRGDVV LAGASFGRVR AMVDENGKQI
QEAGPSIPVE IQGLTEVPAA GDELIALADE RKAREIALFR QGKFRDVKLA RQQAAKLESM
FDNLGEGTQT LPLIVKTDVQ GSQEALVASL TKLSTDEVRV QVVHAAVGGI SESDINLAIA
SNAVVIGFNV RAEQSAKKLA ESNGIDVRYY NIIYDAVDEV KAAMSGMLAP EKKEEVIGLV
EVREVYSISR IGNVAGCMVL DGLVRRDSQI RLLRNNVVHW TGHLDSLRRF KDDVKEVKSG
FDCGLTLRGS NDIQVGDQLE VFEIKEIART L