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 01-MAY-2013, entry version 51.
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; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; 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.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Miller C.D., Anderson A.J., 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
CC which contributes to maintaining a balance among several systems
CC involved in stress resistance and is required for establishment
CC and maintenance of persistent infection in the host. In response
CC to environmental signals MprB acts as both a membrane-associated
CC protein kinase that undergoes autophosphorylation and subsequently
CC transfers the phosphate to MprA, and a protein phosphatase that
CC dephosphorylates phospho-MprA (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC phospho-L-histidine.
CC -!- COFACTOR: Magnesium or manganese (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (Potential).
CC -!- PTM: Autophosphorylated (By similarity).
CC -!- SIMILARITY: Contains 1 HAMP domain.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
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DR EMBL; CP000580; ABO00446.1; -; Genomic_DNA.
DR RefSeq; YP_001072936.1; NC_009077.1.
DR ProteinModelPortal; A3Q5L8; -.
DR STRING; 164757.Mjls_4680; -.
DR EnsemblBacteria; ABO00446; ABO00446; Mjls_4680.
DR GeneID; 4880379; -.
DR KEGG; mjl:Mjls_4680; -.
DR PATRIC; 18095582; VBIMycSp51234_4704.
DR eggNOG; COG0642; -.
DR HOGENOM; HOG000223177; -.
DR KO; K07653; -.
DR OMA; VGGCGVV; -.
DR ProtClustDB; CLSK790870; -.
DR BioCyc; MSP164757:GHV3-4733-MONOMER; -.
DR GO; GO:0016021; C:integral to 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 GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR GO; GO:0023014; P:signal transduction by phosphorylation; IEA:GOC.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_linker_domain.
DR InterPro; IPR003594; HATPase_ATP-bd.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003661; Sig_transdc_His_kin_sub1_dim/P.
DR InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR InterPro; IPR009082; Sig_transdc_His_kinase_dimeric.
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; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF47384; His_kin_homodim; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Kinase;
KW Magnesium; Manganese; Membrane; Nucleotide-binding; Phosphoprotein;
KW Protein phosphatase; Stress response; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1 515 Signal transduction histidine-protein
FT kinase/phosphatase MprB.
FT /FTId=PRO_0000308437.
FT TOPO_DOM 1 24 Cytoplasmic (Potential).
FT TRANSMEM 25 45 Helical; (Potential).
FT TOPO_DOM 46 165 Extracellular (Potential).
FT TRANSMEM 166 186 Helical; (Potential).
FT TOPO_DOM 187 515 Cytoplasmic (Potential).
FT DOMAIN 187 239 HAMP.
FT DOMAIN 247 467 Histidine kinase.
FT MOD_RES 250 250 Phosphohistidine; by autocatalysis (By
FT similarity).
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
//
