UBIB_CELJU
ID UBIB_CELJU Reviewed; 552 AA.
AC B3PH50;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=CJA_3645;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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}.
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DR EMBL; CP000934; ACE85983.1; -; Genomic_DNA.
DR RefSeq; WP_012489220.1; NC_010995.1.
DR AlphaFoldDB; B3PH50; -.
DR SMR; B3PH50; -.
DR STRING; 498211.CJA_3645; -.
DR PRIDE; B3PH50; -.
DR EnsemblBacteria; ACE85983; ACE85983; CJA_3645.
DR KEGG; cja:CJA_3645; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OMA; RRDYKRV; -.
DR OrthoDB; 678616at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001036; 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..552
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000123900"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 118..498
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 124..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 552 AA; 63347 MW; 54B4D38746B0ABC8 CRC64;
MIAFLRLLKI LRVFARYRLD QLLPANLPLA ATLLLLPFKL FPQPRLSRGE RLRRACEDLG
PIFVKFGQLL STRPDLVPAD IVLELNHLQD NVTPFSKGEF QRIVESSLGA SVAEVFASFN
IEPLASASVA QVHTAVLKDG REVVIKVIRP GIDKVIAQDI ALLLRVARWV ENNTLDGKRL
HPVEIVEDYR TTIFDELDLQ REAANGSQLR RNFLNSPLLY VPEVYWEYTR TNVLVMERIY
GIPVTDLAAL NAQQTDMKKL AERGVEIFFT QVFEHNFFHA DMHPGNIFVA HEHPSAPQYI
AVDMAIVGSL TRADQYYLAR NLLAMFRRDY RQVAELHVES GWVPSHVRVE ELEAAVRTVC
EPIFEKPLKE ISFAQVLLNL FRTARRFEME VQPQLVLLQK TLLNIEGLGR QLYPDLDLWA
TAHPFLERWL KNRFHPKSLW RELKRYAPEW MEKFPQVPNL VFNGLQQLQN LGELAPRLEE
ATHAYKAQQQ LARQRNRRRV ITLLAFAGAI ALAWPSLGEG IRHWANHFSF GDIPTASYLL
AAIGLSAWLL KR