UBIB_BURP1
ID UBIB_BURP1 Reviewed; 525 AA.
AC Q3JVZ2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BURPS1710b_0848;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000124; ABA48640.1; -; Genomic_DNA.
DR RefSeq; WP_004189815.1; NC_007434.1.
DR AlphaFoldDB; Q3JVZ2; -.
DR SMR; Q3JVZ2; -.
DR EnsemblBacteria; ABA48640; ABA48640; BURPS1710b_0848.
DR GeneID; 56596665; -.
DR KEGG; bpm:BURPS1710b_0848; -.
DR HOGENOM; CLU_006533_0_0_4; -.
DR OMA; RRDYKRV; -.
DR OrthoDB; 678616at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002700; Chromosome I.
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; Transferase; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT CHAIN 1..525
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000123895"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 118..500
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 285
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 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 525 AA; 59775 MW; 4A181EFE29BC5F5B CRC64;
MRIFRFVKIV FTVIRFGLDE VMLSRIENPR VKLLLRITTI GRRFADPPAV RLRRALESLG
PIFVKFGQVL STRRDLLPVD FANELAKLQD QVPPFDSAVA IAIVEKSLGA RIDVLFDEFE
RVPVASASIA QVHFAKLKQG EHKGKAVAVK VLRPNMLPVI DSDLALMRDI ATWAERLWAD
GRRLKPREVV AEFDKYLHDE LDLMREAANG SQLRRNFAGL DLLLVPEMFW DYSTPAVLVM
ERMTGVPISQ VDTLRAAGVD IPKLAREGVE IFFTQVFRDG FFHADMHPGN IQVSLDPKHF
GRYIALDFGI VGALSDFDKN YLAQNFLAFF KRDYHRVATL HLESGWVPPD TRVEELESAI
RAVCEPYFDR ALKDISLGQV LMRLFSTSRR FNVEIQPQLV LLQKTMLNVE GLGRSLDPEL
DLWKTAKPYL ERWMTEQIGL RGWYERFKVE APQWSKTLPQ LPRLVHQALI SHHEAPRAIS
DDLIRQILVE QRRTNRLLQA LLVFGLAVGA GAVIARVLIV LAYGG