UBIB_SHESR
ID UBIB_SHESR Reviewed; 549 AA.
AC Q0HZP9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, 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=Shewmr7_0403;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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; CP000444; ABI41406.1; -; Genomic_DNA.
DR RefSeq; WP_011624940.1; NC_008322.1.
DR AlphaFoldDB; Q0HZP9; -.
DR SMR; Q0HZP9; -.
DR EnsemblBacteria; ABI41406; ABI41406; Shewmr7_0403.
DR KEGG; shm:Shewmr7_0403; -.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OMA; RRDYKRV; -.
DR OrthoDB; 678616at2; -.
DR UniPathway; UPA00232; -.
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_1000050062"
FT TRANSMEM 498..518
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; 63241 MW; 985CE6B911DB6828 CRC64;
MTLASIRRGY HVIKTLLQYG LDDVLPPKMT PWYFKLARNS LFWIRNKHKG KSGGERLKLA
MQELGPVYIK LGQMLSTRRD LLSDEWANEL AMLQDKVPPF DGALARQAIE AELKAPIESF
FDDFNETPLA SASISQVHTA TLKSNGKAVV LKVLRPNVEA KIQADLLLMS QTAKVIDYLL
GEGNRLRPSE VIEDYRVTIL GELNLKLEAL NAIKLRNNFL DSDALYIPYV YEEFCYPRLM
VMERIYGIPV SDIAALKAQG TNFKLLAERG VELFFTQVFR DNFFHADMHP GNIFISRDHP
ENPYYIGLDC GIMGTLSEVD KRYLAENFLA FFNRDYHRIA QLYIESGWVS EKTDLQAFEQ
AIKVVCEPMF NKPLDEISFG HVLLELFRTA RHFDIVVQPQ LVLLEKTLLY IEGLGRQLYP
QLDLWQTAKP FLEQWMAEQV GPKAMFKKVS TKLPYWSDKL PEFPELIYDN LKLGRKLLSS
QQQMLDKYLK YQQQAHKSNY LLITSAILLI CGTLLFNQDA TLWSPYVCLI SGAALWIIGW
RSRPKNRKF