PRRB_MYCTU
ID PRRB_MYCTU Reviewed; 446 AA.
AC P9WGK7; L0T543; P0A5Z8; Q10560;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Sensor-type histidine kinase PrrB {ECO:0000303|PubMed:14702417};
DE EC=2.7.13.3 {ECO:0000269|PubMed:14702417, ECO:0000269|PubMed:29101285};
GN Name=prrB {ECO:0000303|PubMed:14702417}; OrderedLocusNames=Rv0902c;
GN ORFNames=MTCY31.30c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION.
RC STRAIN=Mt103;
RX PubMed=11953357; DOI=10.1128/iai.70.5.2256-2263.2002;
RA Ewann F., Jackson M., Pethe K., Cooper A., Mielcarek N., Ensergueix D.,
RA Gicquel B., Locht C., Supply P.;
RT "Transient requirement of the PrrA-PrrB two-component system for early
RT intracellular multiplication of Mycobacterium tuberculosis.";
RL Infect. Immun. 70:2256-2263(2002).
RN [3]
RP FUNCTION, AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=Mt103;
RX PubMed=14702417; DOI=10.1099/mic.0.26516-0;
RA Ewann F., Locht C., Supply P.;
RT "Intracellular autoregulation of the Mycobacterium tuberculosis PrrA
RT response regulator.";
RL Microbiology 150:241-246(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, AND INDUCTION BY NITROGEN-LIMITING CONDITIONS.
RX PubMed=22081401; DOI=10.1128/jb.06258-11;
RA Haydel S.E., Malhotra V., Cornelison G.L., Clark-Curtiss J.E.;
RT "The prrAB two-component system is essential for Mycobacterium tuberculosis
RT viability and is induced under nitrogen-limiting conditions.";
RL J. Bacteriol. 194:354-361(2012).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=29101285; DOI=10.1042/bcj20170596;
RA Mishra A.K., Yabaji S.M., Dubey R.K., Dhamija E., Srivastava K.K.;
RT "Dual phosphorylation in response regulator protein PrrA is crucial for
RT intracellular survival of mycobacteria consequent upon transcriptional
RT activation.";
RL Biochem. J. 474:4119-4136(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 (PubMed:11953357,
CC PubMed:22081401). Functions as a sensor protein kinase which is
CC autophosphorylated at a histidine residue and transfers its phosphate
CC group to the conserved aspartic acid residue in the regulatory domain
CC of PrrA (PubMed:14702417, PubMed:29101285). In turn, PrrA binds to the
CC upstream promoter regions of target genes including itself to
CC positively regulate their expression (PubMed:14702417).
CC {ECO:0000269|PubMed:11953357, ECO:0000269|PubMed:14702417,
CC ECO:0000269|PubMed:22081401, ECO:0000269|PubMed:29101285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:14702417,
CC ECO:0000269|PubMed:29101285};
CC -!- INTERACTION:
CC P9WGK7; P9WGK7: prrB; NbExp=7; IntAct=EBI-15568059, EBI-15568059;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By nitrogen-limiting conditions.
CC {ECO:0000269|PubMed:22081401}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:14702417}.
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DR EMBL; AL123456; CCP43650.1; -; Genomic_DNA.
DR PIR; C70783; C70783.
DR RefSeq; NP_215417.1; NC_000962.3.
DR RefSeq; WP_003404689.1; NZ_NVQJ01000001.1.
DR PDB; 1YS3; X-ray; 1.90 A; A/B/C=297-446.
DR PDB; 1YSR; X-ray; 1.78 A; A/B/C=297-446.
DR PDBsum; 1YS3; -.
DR PDBsum; 1YSR; -.
DR AlphaFoldDB; P9WGK7; -.
DR SMR; P9WGK7; -.
DR DIP; DIP-29034N; -.
DR IntAct; P9WGK7; 1.
DR STRING; 83332.Rv0902c; -.
DR PaxDb; P9WGK7; -.
DR DNASU; 885647; -.
DR GeneID; 45424865; -.
DR GeneID; 885647; -.
DR KEGG; mtu:Rv0902c; -.
DR TubercuList; Rv0902c; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; HIEKMQT; -.
DR PhylomeDB; P9WGK7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..446
FT /note="Sensor-type histidine kinase PrrB"
FT /id="PRO_0000074854"
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"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:1YSR"
FT HELIX 306..320
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1YSR"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 373..383
FT /evidence="ECO:0007829|PDB:1YSR"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1YSR"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:1YSR"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:1YSR"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:1YSR"
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
