PRRB_MYCBO
ID PRRB_MYCBO Reviewed; 446 AA.
AC P0A5Z9; A0A1R3XWT7; Q10560; X2BGH8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Sensor-type histidine kinase PrrB;
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P9WGK7};
GN Name=prrB; OrderedLocusNames=BQ2027_MB0926C;
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 [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 [2]
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).
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}.
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DR EMBL; LT708304; SIT99524.1; -; Genomic_DNA.
DR RefSeq; NP_854583.1; NC_002945.3.
DR RefSeq; WP_003404689.1; NC_002945.4.
DR AlphaFoldDB; P0A5Z9; -.
DR SMR; P0A5Z9; -.
DR EnsemblBacteria; SIT99524; SIT99524; BQ2027_MB0926C.
DR GeneID; 45424865; -.
DR PATRIC; fig|233413.5.peg.1007; -.
DR OMA; HIEKMQT; -.
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: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_0000074855"
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