MOXR_PARDE
ID MOXR_PARDE Reviewed; 339 AA.
AC P29901;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein MoxR;
GN Name=moxR;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1657871; DOI=10.1128/jb.173.21.6948-6961.1991;
RA van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H.,
RA Harms N., Oltmann L.F., Stouthamer A.H.;
RT "Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of
RT Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the
RT resultant effect on methylotrophic growth.";
RL J. Bacteriol. 173:6948-6961(1991).
CC -!- FUNCTION: May be involved in the regulation of formation of active
CC methanol dehydrogenase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the MoxR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D41377; D41377.
DR RefSeq; WP_011749267.1; NZ_FOYK01000012.1.
DR AlphaFoldDB; P29901; -.
DR SMR; P29901; -.
DR OMA; PVYEMRR; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011703; ATPase_AAA-3.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07726; AAA_3; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Methanol utilization; Nucleotide-binding.
FT CHAIN 1..339
FT /note="Protein MoxR"
FT /id="PRO_0000096544"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 339 AA; 36923 MW; 9ACFB52B6FE5FC64 CRC64;
MDSNISDWHA RFRDAEAALN GVVLGQARTI RLLLISALCR GHVLLAGDVG TGKTTLLRAM
ARALGGPYGR VEGTVDLLPT DLIYSTHIAE DGRPRIEPGP VLEQGEDMAV FFFNEINRAR
PQVHALLLRL MAERSLSAFR REYRFPHLQV FADRNQIERD ETFELPAAAR DRFLMEIAVD
APAAPEDRVA LAFEPRFHDT TALIAEVGQG ILPYRGLNGL AAGVQSGTHA SPALRRYVFD
LCEALRNPAS AGLALEGADA ARLIRGGVSP RGMQHLVRAA RACAWLEGRE AVLPQDVRAV
LAPVMAHRIF LSPAYEPRRE ALVPALIDAA FATIPVPAA