ID UBIB_SHEB8 Reviewed; 549 AA.
AC A6WIE7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=Shew185_0417;
OS Shewanella baltica (strain OS185).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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}.
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DR EMBL; CP000753; ABS06586.1; -; Genomic_DNA.
DR RefSeq; WP_006087111.1; NC_009665.1.
DR AlphaFoldDB; A6WIE7; -.
DR SMR; A6WIE7; -.
DR GeneID; 11770768; -.
DR KEGG; sbm:Shew185_0417; -.
DR HOGENOM; CLU_006533_0_0_6; -.
DR UniPathway; UPA00232; -.
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; 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_1000050057"
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
//
