ID UBIB_XANOP Reviewed; 557 AA.
AC B2ST34;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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}; OrderedLocusNames=PXO_02769;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(2008).
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; CP000967; ACD61444.1; -; Genomic_DNA.
DR RefSeq; WP_011257293.1; NC_010717.2.
DR AlphaFoldDB; B2ST34; -.
DR SMR; B2ST34; -.
DR KEGG; xop:PXO_02769; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001740; Chromosome.
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..557
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000123932"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 121..509
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 127..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ SEQUENCE 557 AA; 62772 MW; 964D7623F196522E CRC64;
MKAILRASRI GRVILRYRLD ALLEGTPAER WLRLAKPFVP RASAEIAVQS RGARLRLALQ
ELGPIFVKFG QILSTRRDLI PADVAEELTL LQDRVKPFDG EAARLIVERA LGLPVSVAFA
SFDTVPLASA SIAQVHAATL PPDANGVRRE VVVKVLRPEI ERQIDADIAL LHSLATLVER
THPRADKIRP REVVAEIEGT LSAELDLQRE GANASVLRRF WEGSDDLYVP EVIWSHTAER
ALTLERVYGI PSDDIAKLDA AGIDRKALAA KGVRVFYTQV FRDNFFHADA HAGNIWVDSD
PERRLNPRFI ALDFGIMGQL SQEDQYYLAE NFMAIFHKDY RRMAELHVEA GWMPSNVRID
ELEAAARSVC EPYFTRPLSE ISLAQVLIKL FRVAQRYELT LQPQLILLQK TLLNIEGVGR
QLDPKLDIWA VARPVLERIL RERYSPRRVL RELSKRLPEI MTHAPDMPRL VHSWLKQQVE
GRHQIDIRST ELLALDLSLR KLQTRVVTAI TGSGLLVVAA VLYGLHPDGW YLGTVPVWSW
ISGGAGSAAL LVAWLRR
//
