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Database: UniProt
Entry: A0A1G8SWK8_9PSED
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Original site: A0A1G8SWK8_9PSED 
ID   A0A1G8SWK8_9PSED        Unreviewed;       535 AA.
AC   A0A1G8SWK8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Probable protein kinase UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
DE            EC=2.7.-.- {ECO:0000256|HAMAP-Rule:MF_00414};
DE   AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN   Name=ubiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN   ORFNames=SAMN05216186_101170 {ECO:0000313|EMBL:SDJ32940.1};
OS   Pseudomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=137658 {ECO:0000313|EMBL:SDJ32940.1, ECO:0000313|Proteomes:UP000198706};
RN   [1] {ECO:0000313|EMBL:SDJ32940.1, ECO:0000313|Proteomes:UP000198706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21544 {ECO:0000313|EMBL:SDJ32940.1,
RC   ECO:0000313|Proteomes:UP000198706};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_00414}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC       {ECO:0000256|ARBA:ARBA00005020, ECO:0000256|HAMAP-Rule:MF_00414}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00414};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00414}.
CC   -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00414}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00414}.
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DR   EMBL; FNFD01000001; SDJ32940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8SWK8; -.
DR   STRING; 137658.SAMN05216186_101170; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000198706; Unassembled WGS sequence.
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   NCBIfam; TIGR01982; UbiB; 1.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00414}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00414}; Kinase {ECO:0000256|HAMAP-Rule:MF_00414};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00414};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00414}; Reference proteome {ECO:0000313|Proteomes:UP000198706};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00414};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00414};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00414};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_00414}.
FT   TRANSMEM        516..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT   DOMAIN          94..343
FT                   /note="ABC1 atypical kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF03109"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT   BINDING         131..139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   535 AA;  61519 MW;  A715DF4E485B65E4 CRC64;
     MKLLAARRLL RIQSVVIRYR LDDLLLELPL PWWLRTLSYA LPWRWLPRRK THLTRGECLR
     LALEDLGPIF IKFGQLLSTR RDLLPPDIAD ELAKLQDQVP PFDPEQSVAL IESQLGLKVS
     EAFARFDSKP LASASVAQVH AAQLKTGEEV VVKVIRPGLK PIIRQDIAWL FLLAKLAERI
     SAEARRLHPV DVVSDYEKTI YDELDLLREA ANASQLRRNF EDSPLLYVPQ IYWDWCRPKV
     LVMERIYGIP VTDIATLADQ RTDMKLLAER GVEIFFTQVF RDSFFHADMH PGNIFVSTRQ
     PWNPQYIAID CGIVGSLTPE DQDYLARNLV AFFKRDYRKV AQLHIDSGWV PAETKVNEFE
     AAIRTVCEPI FEKPLKEISF GQLLLRLFQT ARRFNMEIQP QLVLLQKTLL NIEGLGRQLY
     PDLDLWTTAQ PFLERWMRER VSPRSLLQNL QAQVEQVPHL AHMTRDLLER MSQPHAADPS
     PPWRERRDDW ALRLIGSILL AGGGTLAASS VTFTSLAAWP AWLMLAAGLV LVVRR
//
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