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UBIB_EDWI9
ID   UBIB_EDWI9              Reviewed;         543 AA.
AC   C5BCA6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=NT01EI_0142;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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; CP001600; ACR67397.1; -; Genomic_DNA.
DR   RefSeq; WP_015869613.1; NC_012779.2.
DR   AlphaFoldDB; C5BCA6; -.
DR   SMR; C5BCA6; -.
DR   STRING; 67780.B6E78_11860; -.
DR   EnsemblBacteria; ACR67397; ACR67397; NT01EI_0142.
DR   GeneID; 7958742; -.
DR   KEGG; eic:NT01EI_0142; -.
DR   PATRIC; fig|634503.3.peg.133; -.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   OrthoDB; 678616at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001485; 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..543
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000206014"
FT   TRANSMEM        517..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          123..501
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        287
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         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   543 AA;  62481 MW;  C7C8671A96BE7B9B CRC64;
     MTPSELRRLC LIIRVFLAYG LDELIPLMRI TLPLRIGRRC LFWMRNRHGD KPLGERLRLA
     LQTLGPVWIK FGQMLSTRRD LFAPAIADQL ALLQDRVAPF DGALARRQIE ASLGGPLEQW
     FDDFDSQALA SASIAQVHTA TLRENGREVV LKVIRPDIQP IIRADVRLMY RLAGWVPKLL
     PDGRRLRPRE VVREYEKTLL DELNLLREAA NAIQLRRNFD ASPMLYIPEV FSDYCRESVL
     VMERIYGVPV SDIAALRAQN TNMKLLAERG VQVFFTQVFR DSFFHADMHP GNIFVSYEHP
     QDPQYIGIDC GIVGSLNKAD KRYLAENFIA FFNRDYRKVA ELHVDSGWVP PDTNIEEFEF
     AIRTVCEPIF EKPLDQISFG HVLLNLFNTA RRFNMEVQPQ LVLLQKTLLY VEGLGRQLYP
     QLDLWTTAKP FLENWLHDQV GLPALMRALK AKAPYWSEKL PELPELLYDS LQQQRRLQHS
     MDSMTHRLGQ QGSRQGRARY LFGIGATLLL SGTILTMVNI ALWPIGLYVA GGVIWLAGWR
     YTR
 
 
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