UBIB_SHEPC
ID UBIB_SHEPC Reviewed; 549 AA.
AC A4Y2Q3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sputcn32_0504;
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 / ATCC BAA-453;
RG US DOE Joint Genome Institute;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-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; CP000681; ABP74236.1; -; Genomic_DNA.
DR RefSeq; WP_011790906.1; NC_009438.1.
DR AlphaFoldDB; A4Y2Q3; -.
DR SMR; A4Y2Q3; -.
DR STRING; 319224.Sputcn32_0504; -.
DR GeneID; 45040940; -.
DR KEGG; spc:Sputcn32_0504; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OMA; RRDYKRV; -.
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_1000050059"
FT TRANSMEM 499..516
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 521..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; 63310 MW; 52023F8F247B293F CRC64;
MTLTSIRRGY HVIKTLLQYG LDEVLPPKMT PWYFTLARSS LFWIRNKHKS KPGGERLKLA
MQELGPVYIK LGQMLSTRRD LLSDEWAIEL AMLQDKVPPF DGVLARKAIE AELKASIESL
FDDFDETPLA SASISQVHTA TLKSNGKAVV LKVLRPNVEA KILADLQLMS QTANLLEYFL
GEGNRLRPAE VIEDYRVTIL GELNLKLEAL NAIKLRNNFL NSDALYVPYV YEEFCYPRLM
VMERIYGIPV SDIAALKAQG TNFKLLAERG VELFFTQVFR DNFFHADMHP GNIFISRDHP
ENPYYIGLDC GIMGTLSEVD KRYLAENFLA FFNRDYHRIA QLYIESGWVS EKTDLQAFEQ
AIKVVCEPMF NKPLDEISFG HVLLELFRTA RSFDIVVQPQ LVLLEKTLLY IEGLGRQLYP
QLDLWQTAKP FLEQWMAEQV GPKAMFKKVS TKLPYWSDKL PEFPELIYDN LKLGRKLLSS
QQQMLDKYLK HQQQAHKSNY MLITSAVLLI CGTLLFNQDA TLWSPYVCLT SGVLMWFIGW
RSRPKNRKF