ID A0A0U1Q2W9_9BURK Unreviewed; 519 AA.
AC A0A0U1Q2W9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AAV94_01600 {ECO:0000313|EMBL:KKW69108.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW69108.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW69108.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW69108.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKW69108.1}.
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DR EMBL; LBNQ01000009; KKW69108.1; -; Genomic_DNA.
DR RefSeq; WP_046740542.1; NZ_LBNQ01000009.1.
DR AlphaFoldDB; A0A0U1Q2W9; -.
DR STRING; 1610491.AAV94_01600; -.
DR PATRIC; fig|1610491.3.peg.328; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000050580; 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:UP000050580};
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:KKW69108.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 495..516
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 88..343
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 126..134
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 519 AA; 59708 MW; E2F64FD7EF35530B CRC64;
MKKFLRGWAI LWVVFRYGLD ELVLTQFRSR PVALLARTLS IGRDLSAPRG QRLREALEQL
GPIFVKFGQV LSTRRDLLPP DIADELARLQ DRVPPFDSAV AVAIIEKAFD GQPIETIFTT
FERTPVASAS IAQVHFATLT DKYGQHHEVA VKVLRPGMLK VIEKDLDLMH MLAGWLEKVS
AEGKRLKPRQ VVAEFDTYLH DELDLMREAA NAAQLRRNMA GLDLVLIPEV FWDYCRTEVM
VMQRMKGVPI SQMETLCARG VDMAQLARDG VTIFFTQVFR DGFFHGDMHP GNIQVSLEPQ
TFGRFISLDF GIVGTLTDFD KEYLAQNFTA FFRRDYKRIA ELHIESGWVP ADTRVAELEA
AVRTVCEPYF DRPLKEISLG MVLMRLFQIS RRFQVEIQPQ LVLLQKTLLN IEGLGRQLDP
DMDLWSTAKP FLEKWMTEQV GPKRFLQELR NEAPRYAQIF PALPRLLHGF LQQQGLGQRE
ELQRLLEEQR RTNRLLGALL PLLLGFLLGV LLMQLYMRW
//
