(data stored in SCRATCH9089 zone)

SWISSPROT: YCHF_PASMU

ID   YCHF_PASMU              Reviewed;         363 AA.
AC   Q9CP90;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; Synonyms=engD;
GN   OrderedLocusNames=PM0163;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC       ribosomal subunit in a nucleotide-independent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_00944}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00944}.
DR   EMBL; AE004439; AAK02247.1; -; Genomic_DNA.
DR   RefSeq; WP_005720428.1; NC_002663.1.
DR   SMR; Q9CP90; -.
DR   PRIDE; Q9CP90; -.
DR   EnsemblBacteria; AAK02247; AAK02247; PM0163.
DR   GeneID; 29389213; -.
DR   KEGG; pmu:PM0163; -.
DR   eggNOG; ENOG4105C3G; Bacteria.
DR   eggNOG; COG0012; LUCA.
DR   HOGENOM; HOG000087629; -.
DR   KO; K06942; -.
DR   OMA; VLRCFDN; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   CDD; cd04867; TGS_YchF_OLA1; 1.
DR   CDD; cd01900; YchF; 1.
DR   Gene3D; 1.10.150.300; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR   InterPro; IPR004396; ATPase_YchF/OLA1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR023192; TGS-like_dom_sf.
DR   InterPro; IPR013029; YchF_C.
DR   InterPro; IPR041706; YchF_N.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF06071; YchF-GTPase_C; 1.
DR   PIRSF; PIRSF006641; CHP00092; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00092; TIGR00092; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CP90.
DR   SWISS-2DPAGE; Q9CP90.
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..363
FT                   /note="Ribosome-binding ATPase YchF"
FT                   /id="PRO_0000201679"
FT   DOMAIN          3..256
FT                   /note="OBG-type G"
FT   DOMAIN          278..361
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   NP_BIND         12..17
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT   METAL           16
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           36
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  39879 MW;  D256C156CE7F8FAF CRC64;
     MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NYPFCTIEPN TGVVPMPDPR LDALAEIVKP
     ERVLPTTMEF VDIAGLVAGA SKGEGLGNKF LANIRETDAI GHVVRCFEND DIVHVAGQIN
     PAEDIDTINT ELALADLDSC ERAIQRLQKR AKGGDKDAKF ELSIMEKILP VLENAGMIRS
     IDLDKDELQA IKGYNFLTLK PTMYIANVNE DGFENNPYLD RVREIAEKEG AVVVPVCAAI
     ESEIAELDDD EKIEFLQDLG IEEPGLNRVI RAGYKLLNLQ TYFTAGVKEV RAWTIPIGAT
     APKSAAVIHT DFEKGFIRAE VIAYDDFIQY KGEAGAKEAG KWRLEGKDYI VQDGDVMHFR
     FNV
//

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