ID   UBIB_SHEB9              Reviewed;         549 AA.
AC   A9KYL6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable protein kinase UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
DE            EC=2.7.-.- {ECO:0000255|HAMAP-Rule:MF_00414};
DE   AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN   Name=ubiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN   OrderedLocusNames=Sbal195_0429;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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:0000255|HAMAP-Rule:MF_00414}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00414}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00414}.
CC   -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000891; ABX47610.1; -; Genomic_DNA.
DR   RefSeq; WP_006087111.1; NC_009997.1.
DR   AlphaFoldDB; A9KYL6; -.
DR   SMR; A9KYL6; -.
DR   EnsemblBacteria; ABX47610; ABX47610; Sbal195_0429.
DR   GeneID; 11770768; -.
DR   KEGG; sbn:Sbal195_0429; -.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000770; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR01982; UbiB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..549
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000080504"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          123..501
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         129..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   549 AA;  63364 MW;  C098DC573E78B2F6 CRC64;
     MTLASIRRGY HVIKTLLQYG LDDVLPPKMT PWYFKLARNS LFWIRNKHKN KPGGERLKLA
     MQELGPVYIK LGQMLSTRRD LLSDEWASEL AMLQDKVPPF DGALARQAIE AELKAPIESL
     FDDFNETPLA SASISQVHTA TLKSNGKDVV LKVLRPNVET KIQADLQLMS QTAKLIEYLL
     GEGNRLRPAE VIEDYRVTIL GELNLKLEAL NAVKLRNNFL DSDALYVPYV YEEFCYPRLM
     VMERIYGISV SDIAALKAQG TNFKLLAERG VELFFTQVFR DNFFHADMHP GNIFISRDHP
     ENPYYIGLDC GIMGTLSEVD KRYLAENFLA FFNRDYHRIA QLYIESGWVS EKTDLQAFEQ
     AIKVVCEPMF NKPLDEISFG HVLLELFRTA RHFDIVVQPQ LVLLEKTLLY IEGLGRQLYP
     QLDLWQTAKP FLEQWMADQV GPKAMFKKVS TKLPYWADKL PEFPELIYDN LKLGRKLLSS
     QQQMLDKYLK YQQQAHKSNY LLITSAVLLI CGTLLINRDA TLWTPYVCLV SGIILWFVGW
     RSRPKNRKF