UBIB_SALTI
ID UBIB_SALTI Reviewed; 546 AA.
AC P0A198; Q9L6M4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; Synonyms=aarF;
GN OrderedLocusNames=STY3587, t3325;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07920.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70853.1; -; Genomic_DNA.
DR RefSeq; NP_457779.1; NC_003198.1.
DR RefSeq; WP_000187559.1; NZ_WSUR01000033.1.
DR AlphaFoldDB; P0A198; -.
DR SMR; P0A198; -.
DR STRING; 220341.16504465; -.
DR EnsemblBacteria; AAO70853; AAO70853; t3325.
DR KEGG; stt:t3325; -.
DR KEGG; sty:STY3587; -.
DR PATRIC; fig|220341.7.peg.3654; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OMA; RRDYKRV; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..546
FT /note="Probable protein kinase UbiB"
FT /id="PRO_0000200717"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 124..502
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 546 AA; 63239 MW; 362873022A808F1A CRC64;
MTPGEVRRLY FIIRTFLSYG LDELIPRMRL TLPLRLWRYS LFWMPNRHKD KLLGERLRLA
LQELGPVWIK FGQMLSTRRD LFPPQIADQL ALLQDKVAPF DGRLAKAQIE EAMGGLPVEA
WFDDFDIQPL ASASIAQVHT ARLKSNGKEV VIKVIRPDIL PVIQADLKLI YRLARWVPRL
LPDGRRLRPT EVVREYEKTL IDELNLLRES ANAIQLRRNF ENSPMLYIPE VYSDYCSQNM
MVMERIYGIP VSDVAALEKN GTNMKLLAER GVKVFFTQVF RDSFFHADMH PGNIFVSHEH
PENPQYIGID CGIVGSLNKE DKRYLAENFI AFFNRDYRKV AELHVDSGWV PPDTNVEDFE
FAIRTVCEPI FEKPLAEISF GHVLLNLFNT ARRFNMEVQP QLVLLQKTLL YVEGVGRQLY
PQLDLWKTAK PFLESWIKDQ VGIPALTRAL KEKAPFWVEK MPEIPELVYD SLRQGKYLQH
SVDKIARELQ VNHVRQSQSR YLLGIGATLL LSGSFLLVNR PEWGLMPGWL MVGGVVVWLV
GWRKTR
