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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
 
 
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