UBIB_PHOPR
ID UBIB_PHOPR Reviewed; 545 AA.
AC Q6LVW8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PBPRA0118;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378663; CAG18557.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6LVW8; -.
DR SMR; Q6LVW8; -.
DR STRING; 298386.PBPRA0118; -.
DR EnsemblBacteria; CAG18557; CAG18557; PBPRA0118.
DR KEGG; ppr:PBPRA0118; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OMA; RRDYKRV; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000593; Chromosome 1.
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..545
FT /note="Probable protein kinase UbiB"
FT /id="PRO_0000200712"
FT TRANSMEM 498..517
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 521..540
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 124..502
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 545 AA; 62988 MW; 0276A370356A22C2 CRC64;
MITPSEFKRL YKIIEVQLRY GLDDFLPEDP RTKMPKMARK SLFWIKNQHP DKSLGERLRL
ALQELGPVWI KFGQMMSTRR DLFPPHIADQ LALLQDQVEP FDGNLAKEHM ELSLGGPIET
WFDDFDETPL ASASIAQVHT ATLKENGREV VLKVIRPDIL PVIQADIKLM YRMAHIVARL
LPEARLLRPV EVVREYEKTL LDELNMMREA ANSIQLRRNF EDSDTLYVPE MFTDYSSTNL
LVMERIYGIQ VSDIDALIAN GTNMKLLSEN AVNIFFTQVF RDSFFHADMH PGNIFVSYEN
PETPQWIALD CGIVGTLNRD DKRYLAENLL AFFHRDYRKV AELHVDSGWV PQDTNIDEFE
FAIRTVCEPI FEKPLCDISF GHVLLNLFNT ARRFDMEVQP QLMLLQKTLL YVEGLGRQLY
PQLDLWITAK PFLEDWMSRQ VGPQAIVEAV KSKAPFWAEK LPELPELLYD SLRQGKVMNQ
RIDKLYDNFM ESRRSQGLAR FYFGIGATLV VCSAILFSNH VETIPVASAA MGVTFWLLGW
RACRK