ID M4RFF0_9ALTE Unreviewed; 543 AA.
AC M4RFF0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Probable protein kinase UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
DE EC=2.7.-.- {ECO:0000256|HAMAP-Rule:MF_00414};
DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN Name=ubiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN ORFNames=C427_0171 {ECO:0000313|EMBL:AGH42281.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH42281.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH42281.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH42281.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
CC -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity which
CC is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC {ECO:0000256|ARBA:ARBA00005020, ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00414};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00414}.
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DR EMBL; CP003837; AGH42281.1; -; Genomic_DNA.
DR RefSeq; WP_015430261.1; NZ_BAES01000046.1.
DR AlphaFoldDB; M4RFF0; -.
DR STRING; 1129794.C427_0171; -.
DR KEGG; gps:C427_0171; -.
DR PATRIC; fig|1129794.4.peg.167; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000011864; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Kinase {ECO:0000256|HAMAP-Rule:MF_00414};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00414};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Reference proteome {ECO:0000313|Proteomes:UP000011864};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 497..514
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT TRANSMEM 520..538
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 90..340
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 127..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ SEQUENCE 543 AA; 62889 MW; 7F6E3F71D40B089F CRC64;
MRILRFYQIN KVMLQHGLDE LIPGKWLPWY AKLGRIGFFW LRNKHPDKSQ GTRVRLALQT
LGPVFIKFGQ MLSTRKDLLP PEVATELSIL QDQVEPFDPE LAKQIILQSL GLEKLSDLFS
EFETKPLASA SIAQVHAAKL KDGNQDVVVK VIRPNIQQTI QSDIELMRTA ASALQKLLPD
GKRLRPVEVV KEYERTIIDE LDLTHEAANG MQFKRNFENS TALYVPTIYS DYSHKNVMVM
ERIYGTPISD IKQLVARNTN MKRLAERGVE VFFTQVFRDS FFHADMHPGN IFVSTVNPND
PQYITIDFGI VGTLNSEDKR YLAENFIAFF NRNYRKVAQL HVDSGWVPSD TDIDDFEASI
RKVCEPIFQK PLAEIEFSNV LLQLFNTARR FNMVIQPQLV LLQKTLLYIE GLGRQLYPQL
DLWKTAKPFL ENWMKEQIGL KAMYQKISTN LPYWSEKLPE IPDLVYDTLK QVKTLPELQK
LQFEAQQEQL RQQHTSTLLM IMGTTFIIIG AILPMYQDNW WPSGCFDLLG LGCWFFAFRK
KRS
//
