ID   MPRB_MYCA1              Reviewed;         522 AA.
AC   A0QBR0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 90.
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=MAV_1095;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-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   -!- SEQUENCE CAUTION:
CC       Sequence=ABK66791.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000479; ABK66791.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_019732008.1; NC_008595.1.
DR   AlphaFoldDB; A0QBR0; -.
DR   SMR; A0QBR0; -.
DR   EnsemblBacteria; ABK66791; ABK66791; MAV_1095.
DR   KEGG; mav:MAV_1095; -.
DR   HOGENOM; CLU_000445_89_6_11; -.
DR   OrthoDB; 692375at2; -.
DR   Proteomes; UP000001574; 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   Stress response; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..522
FT                   /note="Signal transduction histidine-protein
FT                   kinase/phosphatase MprB"
FT                   /id="PRO_0000308431"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..522
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          190..242
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          250..470
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          468..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         253
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   522 AA;  56175 MW;  994010973AD60FCB CRC64;
     MIRLHRPQRP PLRAPLRATP SLSLRWRVML LAMSMVAMVV VLMAFAVYAV ISAALYSDID
     NQLQSRAQLL IASGSLAADP GKAIEGTAYS DVNAMLVNPG HAIYTAQQPG QTLPVGSPEK
     AVIHGELFMS RRTAGDQRIL AVHLQNGTSL LISKSLKPTE AVMNKLRWVL LIVGGVGVAV
     AAVAGGMVTR AGLRPVARLT EAAERVARTD DLRPIPVFGS DELARLTESF NLMLRALAES
     RERQARLVTD AGHELRTPLT SLRTNVELLM ASMEPGAPRL PEQEMVELRA DVLAQIEELS
     TLVGDLVDLT RDDAGQVVHE PVDMSDVIDR SLERVRRRRN DIHFDVDVTP WQMYGDAAGL
     SRAVLNLLDN AAKWSPPGGH VGVTMRQLDP SHAELVVSDH GPGIPPQERR LVFERFYRST
     SARAMPGSGL GLAIVKKVVL NHGGMLRVED TVPGGQPPGT SFYVLLPGRP LPPAGHSTPA
     GESETDKAEA ATDPAVPVAG DTANSRESAN VISVDSQSAR AR