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Database: UniProt
Entry: A0A1N7CI05_9GAMM
LinkDB: A0A1N7CI05_9GAMM
Original site: A0A1N7CI05_9GAMM 
ID   A0A1N7CI05_9GAMM        Unreviewed;       545 AA.
AC   A0A1N7CI05;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN05880558_1218 {ECO:0000313|EMBL:SIR63219.1};
OS   Aeromonas sp. RU39B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIR63219.1, ECO:0000313|Proteomes:UP000186911};
RN   [1] {ECO:0000313|EMBL:SIR63219.1, ECO:0000313|Proteomes:UP000186911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU39B {ECO:0000313|EMBL:SIR63219.1,
RC   ECO:0000313|Proteomes:UP000186911};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTMJ01000021; SIR63219.1; -; Genomic_DNA.
DR   RefSeq; WP_076577571.1; NZ_FTMJ01000021.1.
DR   AlphaFoldDB; A0A1N7CI05; -.
DR   STRING; 1907416.SAMN05880558_1218; -.
DR   InParanoid; A0A1N7CI05; -.
DR   OrthoDB; 9795390at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000186911; 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};
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        498..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT   TRANSMEM        523..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT   DOMAIN          93..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         129..137
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   545 AA;  63011 MW;  C7D885AC52AC2BF7 CRC64;
     MTPQELSRLY QITRILLEHG LDELVPARFQ PWPGRLARRS LFWLKNRSSE RSRGERIRLA
     FEALGPIFIK FGQMLSTRRD LLPPDIAEEL ALLQDRVPPF SGQAARRQIE ESLGATIETL
     FDDFDETPLA SASIAQVHTA RLKENGREIV IKVIRPDIEL VIDADLRLMM TMARWVARIV
     PQSSRLRPVE VVSEYRKTII DELNLMREAA NAIQLRRNFT GSEALYVPEV FTDYCQQQVL
     VMERIYGIPV SDIAALEANG TNMKLLAERG VEVFFTQVFR DSFFHADMHP GNIFVAREHP
     ENPQWIGIDC GIVGTLNRED KRYLAENFLA FFNRDYRRVA ELHVESGWVP ADTKVEEFEF
     AIRTVLEPIF EKPLDQISFG HVLLNLFNTA RRFHMTVQPQ LVLLQKTLLY VEGLGRQLYP
     QLDLWQTAKP FLEHWMREQV GPRAVLNAIR EKAPFWAEKL PELPELVYET LRQTRSQQRH
     FDQLFEQFRQ HSRRQGQARY LLGMGATLLL CSILLHGMAQ PDWAGISLAG AAGCWLIGWI
     KTRTR
//
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