MPRB_MYCBO
ID MPRB_MYCBO Reviewed; 504 AA.
AC Q7U0X3; A0A1R3XX07; Q84BW9; X2BGP2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=BQ2027_MB1008;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG / Pasteur;
RX PubMed=14638785; DOI=10.1128/iai.71.12.6962-6970.2003;
RA Zahrt T.C., Wozniak C., Jones D., Trevett A.;
RT "Functional analysis of the Mycobacterium tuberculosis MprAB two-component
RT signal transduction system.";
RL Infect. Immun. 71:6962-6970(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [4]
RP INDUCTION IN MACROPHAGES.
RC STRAIN=BCG / Pasteur;
RX PubMed=11675502; DOI=10.1073/pnas.221272198;
RA Zahrt T.C., Deretic V.;
RT "Mycobacterium tuberculosis signal transduction system required for
RT persistent infections.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12706-12711(2001).
RN [5]
RP FUNCTION IN MPRA-MEDIATED TRANSCRIPTIONAL REGULATION, AND INDUCTION.
RC STRAIN=BCG / Pasteur;
RX PubMed=15601704; DOI=10.1128/jb.187.1.202-212.2005;
RA He H., Zahrt T.C.;
RT "Identification and characterization of a regulatory sequence recognized by
RT Mycobacterium tuberculosis persistence regulator MprA.";
RL J. Bacteriol. 187:202-212(2005).
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). MprB/MprA up-regulates expression of mprA and pepD.
CC {ECO:0000250, ECO:0000269|PubMed:15601704}.
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 -!- INDUCTION: Induced by MprA. Induced by low concentrations of sodium
CC dodecyl sulfate (SDS). In strain BCG / Pasteur, induced during growth
CC in macrophages. {ECO:0000269|PubMed:11675502,
CC ECO:0000269|PubMed:15601704}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR EMBL; AF490842; AAO85469.1; -; Genomic_DNA.
DR EMBL; LT708304; SIT99607.1; -; Genomic_DNA.
DR RefSeq; NP_854665.1; NC_002945.3.
DR RefSeq; WP_003405123.1; NC_002945.4.
DR AlphaFoldDB; Q7U0X3; -.
DR SMR; Q7U0X3; -.
DR EnsemblBacteria; SIT99607; SIT99607; BQ2027_MB1008.
DR GeneID; 45424951; -.
DR PATRIC; fig|233413.5.peg.1097; -.
DR OMA; VKAQMTE; -.
DR Proteomes; UP000001419; 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 1: Evidence at protein level;
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_0000308432"
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; 54432 MW; 06AD7E74E9549F4A 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 VRRRRNDIHF DVEVIGWQVY GDTAGLSRMA
LNLMDNAAKW SPPGGHVGVR LSQLDASHAE LVVSDRGPGI PVQERRLVFE RFYRSASARA
LPGSGLGLAI VKQVVLNHGG LLRIEDTDPG GQPPGTSIYV LLPGRRMPIP QLPGATAGAR
STDIENSRGS ANVISVESQS TRAT
