UBIB_YERPS
ID UBIB_YERPS Reviewed; 543 AA.
AC Q66FS8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=YPTB0257;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}; Single-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; BX936398; CAH19497.1; -; Genomic_DNA.
DR RefSeq; WP_002211535.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66FS8; -.
DR SMR; Q66FS8; -.
DR EnsemblBacteria; CAH19497; CAH19497; YPTB0257.
DR GeneID; 66843338; -.
DR KEGG; ypo:BZ17_2326; -.
DR KEGG; yps:YPTB0257; -.
DR PATRIC; fig|273123.14.peg.2449; -.
DR OMA; RRDYKRV; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001011; 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..543
FT /note="Probable protein kinase UbiB"
FT /id="PRO_0000200729"
FT TRANSMEM 517..539
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 543 AA; 62427 MW; 105DA2F14519F660 CRC64;
MTPGELRRLY LIIRVFLSYG LDELIPNIRL TLPLRVGRHL FFWLSNRHKD KSLGERLRLA
LQELGPVWIK FGQMMSTRRD LFPPNIADQL ALLQDRVASF DGALARKHIE IAMGGALETW
FDDFDSQALA SASIAQVHTA RLKENGKEVV LKVIRPDILP IIKADVRLMY RLAGWVPKLL
PDGRRLRPRE VVREYEKTLL DELNLLREAA NAIQLRRNFE DSPMLYIPEV YSDYCRESVL
VMERIYGIPV SDIAALEDQG TNMKLLAERG VQVFFTQVFR DSFFHADMHP GNIFVSYEHP
HDPLYIGIDC GIVGSLNKAD KRYLAENFIA FFNRDYRRVA ELHVDSGWVP RDTNVEDFEF
AIRTVCEPIF EKPLAEISFG HVLLNLFNTA RRFNMEVQPQ LVLLQKTLLY VEGLGRQLYP
QLDLWTTAKP FLESWLRDQV GLPAVIRALK EKAPFWAEKF PELPELVYDS LQQHKLLQQS
VEKLTIQIQG QQQRQGQSRY LFGVGATLLV SGTILFLADA TEVSTGFIVA GALAWFIGWR
RTC