MPRB_MYCVP
ID MPRB_MYCVP Reviewed; 484 AA.
AC A1TEL6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase MprB;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
DE AltName: Full=Mycobacterial persistence regulator B;
GN Name=mprB; OrderedLocusNames=Mvan_4843;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system MprB/MprA which
CC contributes to maintaining a balance among several systems involved in
CC stress resistance and is required for establishment and maintenance of
CC persistent infection in the host. In response to environmental signals
CC MprB acts as both a membrane-associated protein kinase that undergoes
CC autophosphorylation and subsequently transfers the phosphate to MprA,
CC and a protein phosphatase that dephosphorylates phospho-MprA (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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; CP000511; ABM15616.1; -; Genomic_DNA.
DR RefSeq; WP_011781990.1; NC_008726.1.
DR AlphaFoldDB; A1TEL6; -.
DR SMR; A1TEL6; -.
DR STRING; 350058.Mvan_4843; -.
DR EnsemblBacteria; ABM15616; ABM15616; Mvan_4843.
DR KEGG; mva:Mvan_4843; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_11; -.
DR OMA; VKAQMTE; -.
DR OrthoDB; 692375at2; -.
DR Proteomes; UP000009159; 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:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Kinase; Magnesium; Manganese;
KW Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Stress response; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..484
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase MprB"
FT /id="PRO_0000308443"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 194..246
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 254..474
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 484 AA; 51961 MW; 8764580DA4F3F44B CRC64;
MAADNAGRWP GQPPGPPAPT HPASSVSLRW RVMLLAMSMV VISVVLMAVA VFAVTSRALY
DDIDNQLRSR AQMLIESRSL DIDPGKAIEG TAYSDMNAMF YIPGRSKYTA NQQGQTLPVG
QPEQDVMDGT LLLSLRTVEH QRVLAIRLAS GNTLLLSKSL APTGKVLKRL GTVLLIVGGL
GVAVAAIAGG MVASAGLRPV GRLTQAAERV ARTDDLRPIP VIGNDELARL TETFNMMLRA
LAESRERQAR LVTDAGHELR TPLTSLRTNV ELLMESMKPG APRIPEEDMA ELRTDVIAQI
EEMSTLVGDL VDLTRDDAGN AVHETVEITE VIDRSLERVR RRRNDIQFDV AVTPWQVYGD
AAGLGRAVLN LLDNAAKWSP PGGRVGVGLT QIDALHAELV VSDRGPGIPP QERALVFERF
FRSTSARSMP GSGLGLAIVK QVVLKHGGTL RIEDTVPGGT PPGTAMHVVL PGRPSPAGSD
EAER
