位置:首页 > 蛋白库 > UBIB_PSEPG
UBIB_PSEPG
ID   UBIB_PSEPG              Reviewed;         540 AA.
AC   B0KM38;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable protein kinase UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
DE            EC=2.7.-.- {ECO:0000255|HAMAP-Rule:MF_00414};
DE   AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN   Name=ubiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN   OrderedLocusNames=PputGB1_5063;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity which
CC       is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00414}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00414}.
CC   -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
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; CP000926; ABZ00948.1; -; Genomic_DNA.
DR   RefSeq; WP_012274570.1; NC_010322.1.
DR   AlphaFoldDB; B0KM38; -.
DR   SMR; B0KM38; -.
DR   STRING; 76869.PputGB1_5063; -.
DR   EnsemblBacteria; ABZ00948; ABZ00948; PputGB1_5063.
DR   KEGG; ppg:PputGB1_5063; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13972; UbiB; 1.
DR   HAMAP; MF_00414; UbiB; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR010232; UbiB.
DR   InterPro; IPR045308; UbiB_bact.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR01982; UbiB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..540
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000080502"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          126..494
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         132..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   540 AA;  61570 MW;  33DA6A8F1A094D9E CRC64;
     MKLLAVRRLF RIQRVVIRYR LDDLLFEQPL LPWWLASLRL LMPWRWLPRK PTELSRGARL
     RLALQDLGPI FIKFGQLLST RRDLLPTDIA DELMLLQDRV PPFDPQKAVA LIEEQLGAKV
     GEVFSRFDVE PLASASVAQV HAARLKTGEE VVVKVVRPGL KPVIAQDLAW LFLIAKAAER
     ASADARRLHP VEIVGDYEKT IYDELDLLRE AANASQLRRN FEGSELMYVP QVYWDLCRPK
     VLVMERIYGV PVTDMVTLAD QRTDMKLLAE RGVEVFFTQV FRDSFFHADM HPGNIFVSTV
     KPWSPQYIAI DCGIVGSLTA EDQDYLARNL IAFFKRDYRR VAQLHIDSGW VPAHTKVNEF
     EAAIRTVCEP IFEKPLKDIS FGQVLMRLFQ TARRFNMEVQ PQLVLLQKTL LNIEGLGRQL
     YPDLDLWSTA KPFLERWMRD RYSPKAVFGN IHGQVEQLPH LANMARDLLE RLSQPHLNDP
     QLPERRRQGD RWALRLLGAG LLGGGAVLAA GAAEAASLAA PAAWPAWLML AAGLYLIVRQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024