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UBIB_HAEDU
ID   UBIB_HAEDU              Reviewed;         542 AA.
AC   Q7VN62;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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}; OrderedLocusNames=HD_0717;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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}; Single-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}.
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DR   EMBL; AE017143; AAP95631.1; -; Genomic_DNA.
DR   RefSeq; WP_010944683.1; NC_002940.2.
DR   AlphaFoldDB; Q7VN62; -.
DR   SMR; Q7VN62; -.
DR   STRING; 233412.HD_0717; -.
DR   PRIDE; Q7VN62; -.
DR   EnsemblBacteria; AAP95631; AAP95631; HD_0717.
DR   KEGG; hdu:HD_0717; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001022; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN           1..542
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_0000200707"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          123..505
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        291
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         129..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   542 AA;  62545 MW;  CA0B5B4C6FEB166B CRC64;
     MIFKNTRRSY QIIATFLRYG IDEIIPDIPF TYSARLTRKA FFWLQNEHKD QPFGVRLRLA
     LQELGPVWIK LGQMLATRRD LFEPALADQL ALLQDSVAPF DGKLARKIIE QALGNTLETW
     FDDFDEQALA SASIAQVHTA TFNKNQPLAG QNVVLKVIRP DIEHIIKADI ALMYQLAKLI
     PYLSDDAKRL RATEVVREYE KTLLDELDLT REMANAIRLR NNFENSEMLY VPAMYPDFCH
     KNVIVMERIY GIPVSDIATL TENGTNMKLL AERGVQVFFT QVFRDSFFHA DMHAGNIFVN
     PNHPEDPQYI GIDCGIVGTL NQNDKRYLAE SFVAFFNRDY RRVALMHIES GWTPADTDVD
     AFEEAFRTVC EPIFAKPLAE ISFGQVLLNL FNVARQFNME VQPQLVLLQK TLLYIEGLGR
     QVYPALDLWQ TAKPFLQKWL DQQVGFKAIL RDLKQQAPQF REHFAQFPEA VFNALQQQKH
     INYRLAELNK TLQSQADNKT YNVKMIIMGS IILSLLWQFN SLPLWLSLPI LTMLCLALCR
     RK
 
 
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