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YCHF_HAEIN
ID   YCHF_HAEIN              Reviewed;         363 AA.
AC   P44681;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 153.
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=HI_0393;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DOMAIN.
RX   PubMed=12837776; DOI=10.1128/jb.185.14.4031-4037.2003;
RA   Teplyakov A., Obmolova G., Chu S.Y., Toedt J., Eisenstein E., Howard A.J.,
RA   Gilliland G.L.;
RT   "Crystal structure of the YchF protein reveals binding sites for GTP and
RT   nucleic acid.";
RL   J. Bacteriol. 185:4031-4037(2003).
RN   [4]
RP   FUNCTION, AND ATPASE ACTIVITY.
RX   PubMed=17430889; DOI=10.1074/jbc.m700541200;
RA   Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., Kostrewa D.,
RA   Kutay U., Kambach C.;
RT   "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding
RT   proteins.";
RL   J. Biol. Chem. 282:19928-19937(2007).
CC   -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC       ribosomal subunit in a nucleotide-independent manner (By similarity).
CC       Does not hydrolyze GTP. {ECO:0000255|HAMAP-Rule:MF_00944,
CC       ECO:0000269|PubMed:17430889}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- DOMAIN: Composed of 3 distinct structural domains: the N-terminal
CC       domain, which has a mononucleotide binding fold typical for the P-loop
CC       NTPases, followed by a pronounced alpha-helical coiled coil domain and
CC       the C-terminal domain, which may be involved in RNA binding.
CC       {ECO:0000269|PubMed:12837776}.
CC   -!- MASS SPECTROMETRY: Mass=40011; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10675023};
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}.
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DR   EMBL; L42023; AAC22052.1; -; Genomic_DNA.
DR   PIR; I64150; I64150.
DR   RefSeq; NP_438555.1; NC_000907.1.
DR   RefSeq; WP_005693776.1; NC_000907.1.
DR   PDB; 1JAL; X-ray; 2.40 A; A/B=1-363.
DR   PDBsum; 1JAL; -.
DR   AlphaFoldDB; P44681; -.
DR   SMR; P44681; -.
DR   STRING; 71421.HI_0393; -.
DR   EnsemblBacteria; AAC22052; AAC22052; HI_0393.
DR   KEGG; hin:HI_0393; -.
DR   PATRIC; fig|71421.8.peg.412; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_6; -.
DR   OMA; VLRCFDN; -.
DR   PhylomeDB; P44681; -.
DR   BioCyc; HINF71421:G1GJ1-408-MON; -.
DR   EvolutionaryTrace; P44681; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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   Gene3D; 3.40.50.300; -; 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-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004095; TGS.
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   1: Evidence at protein level;
KW   3D-structure; 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_0000201678"
FT   DOMAIN          3..256
FT                   /note="OBG-type G"
FT   DOMAIN          278..361
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           15..24
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          98..105
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           121..151
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           156..173
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           185..191
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           217..228
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           238..243
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           267..276
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          279..285
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          287..296
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           301..306
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           312..315
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          318..322
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           324..329
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   HELIX           333..338
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          343..345
FT                   /evidence="ECO:0007829|PDB:1JAL"
FT   STRAND          356..361
FT                   /evidence="ECO:0007829|PDB:1JAL"
SQ   SEQUENCE   363 AA;  39751 MW;  08E00CBEF7D0F65E CRC64;
     MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NYPFCTIEPN TGVVPMPDPR LDALAEIVKP
     ERILPTTMEF VDIAGLVAGA SKGEGLGNKF LANIRETDAI GHVVRCFEND DIVHVAGKID
     PLDDIDTINT ELALADLDSC ERAIQRLQKR AKGGDKEAKF ELSVMEKILP VLENAGMIRS
     VGLDKEELQA IKSYNFLTLK PTMYIANVNE DGFENNPYLD RVREIAAKEG AVVVPVCAAI
     ESEIAELDDE EKVEFLQDLG IEEPGLNRVI RAGYALLNLQ TYFTAGVKEV RAWTVSVGAT
     APKAAAVIHT DFEKGFIRAE VIAYEDFIQF NGENGAKEAG KWRLEGKDYI VQDGDVMHFR
     FNV
 
 
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