ID A0A0W0R0M9_9GAMM Unreviewed; 550 AA.
AC A0A0W0R0M9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:KTC64630.1};
GN Synonyms=aarF {ECO:0000313|EMBL:VEH86098.1};
GN ORFNames=Lade_1924 {ECO:0000313|EMBL:KTC64630.1}, NCTC12735_01745
GN {ECO:0000313|EMBL:VEH86098.1};
OS Legionella adelaidensis.
OG Plasmid 24 {ECO:0000313|EMBL:VEH86098.1,
OG ECO:0000313|Proteomes:UP000281170}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC64630.1, ECO:0000313|Proteomes:UP000054859};
RN [1] {ECO:0000313|EMBL:KTC64630.1, ECO:0000313|Proteomes:UP000054859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC64630.1,
RC ECO:0000313|Proteomes:UP000054859};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Identification of large and diverse effector repertoires of 38 Legionella
RT species.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEH86098.1, ECO:0000313|Proteomes:UP000281170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH86098.1,
RC ECO:0000313|Proteomes:UP000281170};
RC PLASMID=24 {ECO:0000313|Proteomes:UP000281170};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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 Multi-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; LNKA01000019; KTC64630.1; -; Genomic_DNA.
DR EMBL; LR134433; VEH86098.1; -; Genomic_DNA.
DR RefSeq; WP_058462987.1; NZ_LR134433.1.
DR AlphaFoldDB; A0A0W0R0M9; -.
DR STRING; 45056.Lade_1924; -.
DR KEGG; ladl:NCTC12735_01745; -.
DR PATRIC; fig|45056.6.peg.1985; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000054859; Unassembled WGS sequence.
DR Proteomes; UP000281170; Plasmid 24.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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}; Plasmid {ECO:0000313|EMBL:VEH86098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054859};
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}; Ubiquinone {ECO:0000313|EMBL:KTC64630.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 497..521
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT TRANSMEM 527..544
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 93..342
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ SEQUENCE 550 AA; 63738 MW; B7C3BD0CFC286E17 CRC64;
MKSTKQLFRL LRINYVLTKN GLDQVILSIR LFAPFRFIAY FNPWNWFRKE KLTRGQAIRK
TLEELGPIFI KFGQALSTRP DILPPDIALE LSKLQDQVPP FPSEQALAIL ESAFGHSAHE
VFAQFDEEVL ASASMAQVHA ATLKTGEDVV VKILRPNMRK VIEQDLSILY TIAHLAERYW
AESKRLKPKE IVKEFEKTLF DELNLQREAA NASQLRRNFN NSPLLYVPEI YWDYVRENVI
VMERIYGIPV TDITALKENG VNIKKLAERG LQIFFTQVFR DCFFHADMHP GNIFVSFENP
EDPQYICVDF GIIGTLSEND KRYIAENLLA FFNRDYRRVA QLHVESGWVA RDTHVEEFES
AIRTVSEPIF ERPLKDISFA LLVMQLFQVA RRFNMQVQPQ LVLLQKTLLA IEGLGRQLYP
DLDLWTTGKP FLEKWVKEQM GPQAFFQHLR ANLPFFIEQL PHMPKLFNDV LLLTKEQKIQ
EIEKNLLRGP LKLSKFAWYK GLGAGVFVVM MLFSGLSYFN VLEPDKLATA ALITAFAGGL
LSFWSRRKRR
//
