ID   UBIB_XANAC              Reviewed;         557 AA.
AC   Q8PQT0;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=XAC0242;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35134.1; -; Genomic_DNA.
DR   RefSeq; WP_011050186.1; NC_003919.1.
DR   AlphaFoldDB; Q8PQT0; -.
DR   SMR; Q8PQT0; -.
DR   STRING; 190486.XAC0242; -.
DR   EnsemblBacteria; AAM35134; AAM35134; XAC0242.
DR   GeneID; 66909454; -.
DR   KEGG; xac:XAC0242; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000576; 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..557
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_0000200724"
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;  62634 MW;  B40E3067968E0E4C CRC64;
     MKAILRASRI GRVILRYRLD ALLEGTPAER WLRLAKPFVP RASAEIAAQS RGARLRLALQ
     ELGPIFVKFG QILSTRRDLI PADVAEELTL LQDRVKPFDG QAARLIVEAA LGLPVSVAFA
     SFDTVPLASA SIAQVHAATL PPDANGVRRE VVVKVLRPEI ERQIDADIAL LHSLATLVER
     THPRADKIRP REVVAEIEGT LAAELDLQRE GANASVLRRF WEGSDDLYVP EVIWSHTAER
     ALTLERVYGI PSDDIAKLDA AGIDRKALAA KGVRVFYTQV FRDNFFHADA HAGNIWVDSD
     PERRLNPRFI ALDFGIMGQL SQEDQYYLAE NFMAIFHKDY RRMAELHVEA GWMPSNVRID
     ELEAAARSVC EPYFNRPLSE ISLAQVLIKL FRVAQRYELT LQPQLILLQK TLLNIEGVGR
     QLDPRLDIWA VARPVLERIL RERYSPRRVL RELSKRLPEI MTHAPDMPRL VYSWLTQQVE
     GRHQIAIRSP ELLALDLSLR KLQTRVVTAI TGSGLLVVAA VLYGLHPDGW YLGTVPVWSW
     ISGGAGSAAL LVAWLRR