UBIB_ACIAC
ID UBIB_ACIAC Reviewed; 522 AA.
AC A1TTA2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Aave_3641;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) 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; CP000512; ABM34190.1; -; Genomic_DNA.
DR RefSeq; WP_011796687.1; NC_008752.1.
DR AlphaFoldDB; A1TTA2; -.
DR SMR; A1TTA2; -.
DR STRING; 397945.Aave_3641; -.
DR EnsemblBacteria; ABM34190; ABM34190; Aave_3641.
DR KEGG; aav:Aave_3641; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_4; -.
DR OMA; RRDYKRV; -.
DR OrthoDB; 678616at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002596; 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..522
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000123885"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 119..497
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 125..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 522 AA; 60351 MW; 19AD63FE6AFCE623 CRC64;
MSRLFRGATI VWVVLRYGLD ELVLTSFQKP WLRLLARIVS FGRKLDAPRG QRLREALERL
GPIFVKFGQV LSTRRDLLPP DIANELALLQ DRVPPFDPDV AVATIERAFR RPVGEVFVSF
ERVPVASASI AQVHFAIVRD RHGVEREVAV KVLRPGMLPV IDNDLGLMRA MAGWVESLSA
DGKRLKPRQV VAEFDNYLHD ELDLIREAAN AAQLRRNMER LGLVRIPEIL WDFCHPEVLV
MERMKGVPIS QIERLRAAGV DIRQLARDGV TIFFTQVFRD GFFHADMHPG NIQVSLEPGS
FGRYISLDFG IVGSLTEFDK EYLAQNFTAF FRRDYKRVAE LHVESGWVPA DTRINELESA
IRAVCEPYFD RPLKEISLGM VLMRLFQTSR RFHVEIQPQL VLLQKTLLNI EGLGRQLDPE
LDLWSTAKPF LEKWMLDQMG PQRLWREVKA ESPHFAKMLP ELPRLLHDYL HHKPHDHRRE
MQELLAEQRR TNRLLQSIIY GGMGFVLGLL ALQFLIRIRF FH