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Database: UniProt
Entry: I2JPV1_9GAMM
LinkDB: I2JPV1_9GAMM
Original site: I2JPV1_9GAMM 
ID   I2JPV1_9GAMM            Unreviewed;       546 AA.
AC   I2JPV1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=DOK_00537 {ECO:0000313|EMBL:EIF45003.1};
OS   gamma proteobacterium BDW918.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae.
OX   NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF45003.1, ECO:0000313|Proteomes:UP000003473};
RN   [1] {ECO:0000313|EMBL:EIF45003.1, ECO:0000313|Proteomes:UP000003473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDW918 {ECO:0000313|EMBL:EIF45003.1,
RC   ECO:0000313|Proteomes:UP000003473};
RX   PubMed=22740675; DOI=10.1128/JB.00678-12;
RA   Kim S.M., Cho S.J., Lee S.B.;
RT   "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL   J. Bacteriol. 194:3753-3754(2012).
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   -!- 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: 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:EIF45003.1}.
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DR   EMBL; AJMK01000002; EIF45003.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2JPV1; -.
DR   PATRIC; fig|1168065.3.peg.115; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OrthoDB; 9795390at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000003473; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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:UP000003473};
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   DOMAIN          89..339
FT                   /note="ABC1 atypical kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF03109"
FT   ACT_SITE        283
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         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   546 AA;  62404 MW;  078AD921B25DE873 CRC64;
     MGLRRLLAIC WIICVYRLDT LIPTEHLPLR ARLLLRCGPW RLFAKGKYSR GERLRLGLEN
     LGPIFIKFGQ ILSTRRDLLA DDVAMELAKL QDQVPPFGSE QAVAVIEAAL GKPIEQLFLK
     FDRQPLASAS IAQVHTATID NNIDVVVKVV RPGIEHIISA DLKLLQTIAV LIARYIPDGR
     RLRPVEVVED YRHTILDELD LQREGANTSQ LRRNFKDSEV LYVPEVYWDY TRRNILVMER
     IYGIPVTDVE TLKEQGTDMK KLAERGVEIF FTQVFRDSFF HADMHPGNIF IAHNRPNSPQ
     YIAIDCAIIG SLSDFDQYYL ARNLLAIFQR NYREVAELHI ECGWVPPETR VHEFEAAIRT
     VSEPIFEKPL AEISFGLLLL QLFQTARRFD MEVQPSLVLL QKTLLNIEGL GRQLYPQLDL
     WSTAMPFLER WVRDRYSPQS VLKKVSHRIP GWLEQLPNLP EALLERGGAG KEQISANTKA
     ERQLQHDFAE MIKQQAQRGR NQRLAIVAAL AAALVSDPGI RAGLQELPSM SIGLFAVALY
     FFIRSR
//
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