MPRB_MYCTO
ID MPRB_MYCTO Reviewed; 504 AA.
AC P9WGL0; L0T8A3; O53895; Q7D913;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
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=MT1010;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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. MprB/MprA
CC is involved in regulation of numerous stress-responsive genes (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}.
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DR EMBL; AE000516; AAK45258.1; -; Genomic_DNA.
DR PIR; B70821; B70821.
DR RefSeq; WP_003911317.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGL0; -.
DR SMR; P9WGL0; -.
DR EnsemblBacteria; AAK45258; AAK45258; MT1010.
DR KEGG; mtc:MT1010; -.
DR PATRIC; fig|83331.31.peg.1084; -.
DR HOGENOM; CLU_000445_89_6_11; -.
DR Proteomes; UP000001020; 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..504
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase MprB"
FT /id="PRO_0000428343"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 186..238
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 246..466
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 471..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 504 AA; 54408 MW; 26792A71AC432232 CRC64;
MWWFRRRDRA PLRATSSLSL RWRVMLLAMS MVAMVVVLMS FAVYAVISAA LYSDIDNQLQ
SRAQLLIASG SLAADPGKAI EGTAYSDVNA MLVNPGQSIY TAQQPGQTLP VGAAEKAVIR
GELFMSRRTT ADQRVLAIRL TNGSSLLISK SLKPTEAVMN KLRWVLLIVG GIGVAVAAVA
GGMVTRAGLR PVGRLTEAAE RVARTDDLRP IPVFGSDELA RLTEAFNLML RALAESRERQ
ARLVTDAGHE LRTPLTSLRT NVELLMASMA PGAPRLPKQE MVDLRADVLA QIEELSTLVG
DLVDLSRGDA GEVVHEPVDM ADVVDRSLER VRRRRNDILF DVEVIGWQVY GDTAGLSRMA
LNLMDNAAKW SPPGGHVGVR LSQLDASHAE LVVSDRGPGI PVQERRLVFE RFYRSASARA
LPGSGLGLAI VKQVVLNHGG LLRIEDTDPG GQPPGTSIYV LLPGRRMPIP QLPGATAGAR
STDIENSRGS ANVISVESQS TRAT
