MPRB_MYCSJ
ID MPRB_MYCSJ Reviewed; 515 AA.
AC A3Q5L8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Mjls_4680;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) 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}.
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DR EMBL; CP000580; ABO00446.1; -; Genomic_DNA.
DR AlphaFoldDB; A3Q5L8; -.
DR SMR; A3Q5L8; -.
DR STRING; 164757.Mjls_4680; -.
DR KEGG; mjl:Mjls_4680; -.
DR HOGENOM; CLU_000445_89_6_11; -.
DR OMA; VKAQMTE; -.
DR BioCyc; MSP164757:G1G8C-4723-MON; -.
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..515
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase MprB"
FT /id="PRO_0000308437"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 187..239
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 247..467
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 468..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 515 AA; 55042 MW; C6F03726FD719518 CRC64;
MTLPPQPSRL KPPRNTSSLS LRWRVMLLAM SMVAMVVVLM SVAVYAVVSR ALYDDIDNQL
HSRARLLIES GSLAADPGKA IEGTAYSDVN AMLVNPGRSI YTANQQGQTL PLGEAEKDVI
SGELLLSLRT ANHQRILAVH LTNGSSLLIS KSLAPTGQVL GRLGTVLLIV GGVGVAVAAI
AGGMVARAGL RPVGRLTQAA ERVARTDDLR PIPVFGSDEL ARLTEAFNMM LRALTESRER
QARLVSDAGH ELRTPLTSLR TNVELLMASQ APGAPRLPEE EMAGLRADVI AQIEELSTLV
GDLVDLTRDE AGGVVYETVD MAEVVDRSLE RVRRRRNDIE FDVNVVGWQV YGDAAGLARA
VLNLLDNAAK WSPPGGRVGV RLTQTDPVHA ELVVSDQGPG IPEAERRLVF ERFYRSTAAR
AMPGSGLGLA IVKQVVLKHG GALRVEDTVP GGNPPGTSFY VMLPGRPLTP GGNGTAPVPA
AQFDPDMRSA GSRADRRVIK NTETNGKSRS ASKEL
