ID   PRRB_MYCTO              Reviewed;         446 AA.
AC   P9WGK6; L0T543; P0A5Z8; Q10560;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Sensor-type histidine kinase PrrB;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P9WGK7};
GN   Name=prrB; OrderedLocusNames=MT0925;
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 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   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45172.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70783; C70783.
DR   RefSeq; WP_003404689.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGK6; -.
DR   SMR; P9WGK6; -.
DR   EnsemblBacteria; AAK45172; AAK45172; MT0925.
DR   GeneID; 45424865; -.
DR   KEGG; mtc:MT0925; -.
DR   PATRIC; fig|83331.31.peg.994; -.
DR   HOGENOM; CLU_026160_0_0_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: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; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..446
FT                   /note="Sensor-type histidine kinase PrrB"
FT                   /id="PRO_0000428345"
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;  47829 MW;  CD84A335CCFFE6D7 CRC64;
     MNILSRIFAR TPSLRTRVVV ATAIGAAIPV LIVGTVVWVG ITNDRKERLD RRLDEAAGFA
     IPFVPRGLDE IPRSPNDQDA LITVRRGNVI KSNSDITLPK LQDDYADTYV RGVRYRVRTV
     EIPGPEPTSV AVGATYDATV AETNNLHRRV LLICTFAIGA AAVFAWLLAA FAVRPFKQLA
     EQTRSIDAGD EAPRVEVHGA SEAIEIAEAM RGMLQRIWNE QNRTKEALAS ARDFAAVSSH
     ELRTPLTAMR TNLEVLSTLD LPDDQRKEVL NDVIRTQSRI EATLSALERL AQGELSTSDD
     HVPVDITDLL DRAAHDAARI YPDLDVSLVP SPTCIIVGLP AGLRLAVDNA IANAVKHGGA
     TLVQLSAVSS RAGVEIAIDD NGSGVPEGER QVVFERFSRG STASHSGSGL GLALVAQQAQ
     LHGGTASLEN SPLGGARLVL RLPGPS