ID   PRRB_MYCLE              Reviewed;         446 AA.
AC   O33071;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=Sensor-type histidine kinase PrrB;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P9WGK7};
GN   Name=prrB; OrderedLocusNames=ML2124; ORFNames=MLCB57.60c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system PrrB/PrrA that
CC       is involved specifically in early intracellular multiplication of
CC       Mycobacterium and is essential for its viability. Functions as a sensor
CC       protein kinase which is autophosphorylated at a histidine residue and
CC       transfers its phosphate group to the conserved aspartic acid residue in
CC       the regulatory domain of PrrA. In turn, PrrA binds to the upstream
CC       promoter regions of target genes including itself to positively
CC       regulate their expression. {ECO:0000250|UniProtKB:P9WGK7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P9WGK7};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P9WGK7}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z99494; CAB16700.1; -; Genomic_DNA.
DR   EMBL; AL583924; CAC31079.1; -; Genomic_DNA.
DR   PIR; T45358; T45358.
DR   RefSeq; NP_302403.1; NC_002677.1.
DR   RefSeq; WP_010908723.1; NC_002677.1.
DR   AlphaFoldDB; O33071; -.
DR   SMR; O33071; -.
DR   STRING; 272631.ML2124; -.
DR   EnsemblBacteria; CAC31079; CAC31079; CAC31079.
DR   KEGG; mle:ML2124; -.
DR   PATRIC; fig|272631.5.peg.4010; -.
DR   Leproma; ML2124; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_026160_0_0_11; -.
DR   OMA; HIEKMQT; -.
DR   Proteomes; UP000000806; 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: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; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..446
FT                   /note="Sensor-type histidine kinase PrrB"
FT                   /id="PRO_0000074853"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          172..222
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          237..446
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         240
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   446 AA;  47796 MW;  C1F3F7AD8E07ED80 CRC64;
     MNILSRIFAR TPSLRTRVVV ATAIGAAIPV LIVGTVVWVG ITNDRKERLD RKLDEAAGFA
     IPFVPRGLDE IPRSPNDQDA IITVRRGNLV KSNFDITLPK LTNDYADTYL RGVRYRVRTV
     EIPAPEPTSI AVGATYDATV AETNNLHRRV LLICGFAIAA AAVFAWLLAA FAVRPFKQLA
     QQTRSVDAGG EAPRVEVHGA TEAVEIAEAM RGMLQRIWNE QNRTKEALAS ARDFAAVSSH
     ELRTPLTAMR TNLEVLATLD LADDQRKEVL GDVIRTQSRI EATLSALERL AQGELSTSDD
     HVPVDITELL DRAAHDATRS YPELKVSLVP SPTCIIVGLP AGLRLAVDNA VANAVKHGGA
     TRVQLSAVSS RAGVEIAVDD NGSGVPEDER QVVFERFSRG STASHSGSGL GLALVAQQAQ
     LHGGTASLET SPLGGARLLL RISAPS