(data stored in ACNUC7421 zone)

SWISSPROT: UBIB_PSEPF

ID   UBIB_PSEPF              Reviewed;         534 AA.
AC   Q3KJC7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
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=Pfl01_0385;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity
CC       which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis
CC       [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}.
DR   EMBL; CP000094; ABA72129.1; -; Genomic_DNA.
DR   RefSeq; WP_011332063.1; NC_007492.2.
DR   SMR; Q3KJC7; -.
DR   STRING; 205922.Pfl01_0385; -.
DR   PRIDE; Q3KJC7; -.
DR   EnsemblBacteria; ABA72129; ABA72129; Pfl01_0385.
DR   KEGG; pfo:Pfl01_0385; -.
DR   eggNOG; ENOG4105CNK; Bacteria.
DR   eggNOG; COG0661; LUCA.
DR   HOGENOM; HOG000264440; -.
DR   KO; K03688; -.
DR   OMA; DFGMMDQ; -.
DR   BioCyc; PFLU205922:G1G4S-389-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002704; 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: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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR010232; UbiB.
DR   InterPro; IPR004147; UbiB_dom.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR01982; UbiB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJC7.
DR   SWISS-2DPAGE; Q3KJC7.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Kinase; Membrane; Nucleotide-binding; Transferase; Transmembrane;
KW   Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN         1    534       Probable protein kinase UbiB.
FT                                /FTId=PRO_1000050051.
FT   TRANSMEM     23     43       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00414}.
FT   TRANSMEM    490    510       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00414}.
FT   TRANSMEM    512    532       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00414}.
FT   DOMAIN      125    492       Protein kinase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00414}.
FT   NP_BIND     131    139       ATP. {ECO:0000255|HAMAP-Rule:MF_00414}.
FT   ACT_SITE    288    288       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00414}.
FT   BINDING     153    153       ATP. {ECO:0000255|HAMAP-Rule:MF_00414}.
SQ   SEQUENCE   534 AA;  61507 MW;  1C9BF47FFA33037E CRC64;
     MKLLAVRRLL RIQRVVIRYR LDDLLFDLPL PWFLLALRYV LPWRWFPRKP LELSRGARLR
     LALQDLGPIF IKFGQILSTR RDLLPEDIAD ELMRLQDRVP PFDSQLSVKL IEEQLGKKIS
     EVFSRFDVEP LASASVAQVH AAQLKTGEEV VVKVIRPGLK PIIAQDLAWL FILARAAEKV
     SADARLLHPV DVVSDYEKTI YDELDLLREA ANASQLKRNF EGSPLLYVPQ VYWDWCRPKV
     LVMERIYGIQ VTDLATLADQ RTDMKMLAER GVEIFFTQVF RDSFFHADMH PGNIFVSTVN
     PWSPQYIAID CGIVGSLTPE DQDYLARNLF AFFKRDYRRV AQLHIDSGWV PAETKLNEFE
     AAIRTVCEPI FEKPLKDISF GQVLMRLFQT ARRFNMEVQP QLVLLQKTLL NIEGLGRQLY
     PDLDLWNTAQ PFLERWMRER VSPKALLGNV QSQFEQLPHL ANMARDLLER MSQPHANDPP
     PPWKKRKDDW FLRLLGSAHL AGGTILAAGG PLHELGHWPA GIMVAVGLYL VVRR
//

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