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UBIB_SERP5
ID   UBIB_SERP5              Reviewed;         543 AA.
AC   A8G8C0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Spro_0250;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV39360.1; -; Genomic_DNA.
DR   RefSeq; WP_012004720.1; NC_009832.1.
DR   AlphaFoldDB; A8G8C0; -.
DR   SMR; A8G8C0; -.
DR   STRING; 399741.Spro_0250; -.
DR   EnsemblBacteria; ABV39360; ABV39360; Spro_0250.
DR   KEGG; spe:Spro_0250; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   OrthoDB; 678616at2; -.
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..543
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000060070"
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   TRANSMEM        519..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;  62604 MW;  76F176E6A785FA59 CRC64;
     MTPGELRRLY LIVRVFLSYG LDELIPQMRL TLPLRVGRRL LFWMPNRHAD KPLGERLRLA
     LQELGPVWIK FGQMMSTRRD LFPPQIADQL TLLQDRVAPF DGALARKHIE LAMGGPLETW
     FDDFDQQALA SASIAQVHTA RLKTTGQEVV LKVIRPDIRP IIKADVRLMY RLAAWVPKLM
     PDGRRLRPRE VVREYEKTLL DELNLLREAA NAIQLRRNFD GSPMLYVPEV YSDYCRESVL
     VMERIYGIPV SDIPTLEKQG TNMKLLAERG VQVFFTQVFR DSFFHADMHP GNIFVSYEHP
     EDPCYIGIDC GIVGSLNKDD KRYLAENFIA FFNRDYRKVA ELHVDSGWVP RDTNVEDFEF
     AIRTVCEPIF EKPLSEISFG NVLLNLFNTA RRFNMEVQPQ LVLLQKTLLY VEGLGRQLYP
     QLDLWTTAKP FLESWMRDQV GIPAVIRALK EKAPFWAEKL PELPELFYDS LQQHKLLQQS
     VDKLTNQMQA QRVRQGQSRY LFGVGATLLV SGTILLSGDV EVFPAWLIAA GIVSWVIGWK
     RTT
 
 
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