PRPR_MYCTU
ID PRPR_MYCTU Reviewed; 486 AA.
AC O06581; F2GGE3; I6XX54; Q7D8T0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=HTH-type transcriptional regulator PrpR {ECO:0000303|PubMed:22365605};
DE AltName: Full=Propionate regulator {ECO:0000303|PubMed:22916289};
DE Short=PRPR {ECO:0000303|PubMed:22916289};
GN Name=prpR {ECO:0000303|PubMed:22916289};
GN OrderedLocusNames=Rv1129c, RVBD_1129c; ORFNames=P425_01178;
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, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=22365605; DOI=10.1016/j.chembiol.2011.12.016;
RA Griffin J.E., Pandey A.K., Gilmore S.A., Mizrahi V., McKinney J.D.,
RA Bertozzi C.R., Sassetti C.M.;
RT "Cholesterol catabolism by Mycobacterium tuberculosis requires
RT transcriptional and metabolic adaptations.";
RL Chem. Biol. 19:218-227(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=22916289; DOI=10.1371/journal.pone.0043651;
RA Masiewicz P., Brzostek A., Wolanski M., Dziadek J.,
RA Zakrzewska-Czerwinska J.;
RT "A novel role of the PrpR as a transcription factor involved in the
RT regulation of methylcitrate pathway in Mycobacterium tuberculosis.";
RL PLoS ONE 7:E43651-E43651(2012).
RN [7]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=24705740; DOI=10.1007/s10482-014-0153-0;
RA Masiewicz P., Wolanski M., Brzostek A., Dziadek J.,
RA Zakrzewska-Czerwinska J.;
RT "Propionate represses the dnaA gene via the methylcitrate pathway-
RT regulating transcription factor, PrpR, in Mycobacterium tuberculosis.";
RL Antonie Van Leeuwenhoek 105:951-959(2014).
CC -!- FUNCTION: Plays a key role in regulating expression of enzymes involved
CC in the catabolism of short chain fatty acids (SCFA) via both the
CC glyoxylate (acetyl degradation route) and the methylcitrate cycle
CC (propionate degradation route) (PubMed:22916289, PubMed:24705740).
CC Required for intracellular growth in macrophages and for the
CC assimilation of cholesterol-derived propionate (PubMed:22365605). PrpR
CC acts as a transcriptional activator of prpDC and icl genes when
CC propionate is the main carbon source, and as a ramB repressor
CC (PubMed:22916289). During growth on propionate, PrpR also acts as a
CC transcriptional repressor of dnaA, which encodes the DnaA initiator
CC protein responsible for initiating chromosomal replication
CC (PubMed:24705740). It is possibly involved in the regulation of genes
CC responsible for controlling cholesterol utilization (PubMed:22365605).
CC {ECO:0000269|PubMed:22365605, ECO:0000269|PubMed:22916289,
CC ECO:0000269|PubMed:24705740}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:22365605}.
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000305|PubMed:22365605, ECO:0000305|PubMed:22916289}.
CC -!- INDUCTION: By propionate. {ECO:0000269|PubMed:22916289}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow using
CC either propionate or cholesterol as a primary carbon source and the
CC transcript levels of both prpD and prpC are dramatically reduced
CC regardless of carbon source. When the mutant grows on medium containing
CC glucose or acetate as a sole carbon source, there is no significant
CC difference in growth compared to the wild-type.
CC {ECO:0000269|PubMed:22365605, ECO:0000269|PubMed:22916289}.
CC -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC regulator (ScfR) family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43883.1; -; Genomic_DNA.
DR EMBL; CP003248; AFN49028.1; -; Genomic_DNA.
DR EMBL; JLDD01000012; KBJ36375.1; -; Genomic_DNA.
DR RefSeq; NP_215645.1; NC_000962.3.
DR RefSeq; WP_003405904.1; NZ_NVQJ01000021.1.
DR PDB; 6CYJ; X-ray; 2.70 A; A/B=81-486.
DR PDB; 6CYY; X-ray; 2.51 A; A/B=81-486.
DR PDB; 6CZ6; X-ray; 2.70 A; A/B/C/D=81-486.
DR PDB; 6D2S; X-ray; 1.82 A; A=155-440.
DR PDBsum; 6CYJ; -.
DR PDBsum; 6CYY; -.
DR PDBsum; 6CZ6; -.
DR PDBsum; 6D2S; -.
DR AlphaFoldDB; O06581; -.
DR SMR; O06581; -.
DR STRING; 83332.Rv1129c; -.
DR PaxDb; O06581; -.
DR PRIDE; O06581; -.
DR DNASU; 885963; -.
DR GeneID; 885963; -.
DR KEGG; mtu:Rv1129c; -.
DR KEGG; mtv:RVBD_1129c; -.
DR PATRIC; fig|83332.111.peg.1261; -.
DR TubercuList; Rv1129c; -.
DR eggNOG; COG1396; Bacteria.
DR eggNOG; COG3800; Bacteria.
DR OMA; RRFDRHS; -.
DR PhylomeDB; O06581; -.
DR UniPathway; UPA00296; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR026281; HTH_RamB.
DR InterPro; IPR010359; IrrE_HExxH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR018653; ScfR_C.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF06114; Peptidase_M78; 1.
DR Pfam; PF09856; ScfRs; 1.
DR PIRSF; PIRSF019251; Rv0465c; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..486
FT /note="HTH-type transcriptional regulator PrpR"
FT /id="PRO_0000433054"
FT DOMAIN 22..76
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 33..52
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:6D2S"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6D2S"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:6D2S"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6CYY"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:6D2S"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6D2S"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:6CYY"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6CYY"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6CYY"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:6CYY"
SQ SEQUENCE 486 AA; 54087 MW; 6F3CD3C041A1DEBB CRC64;
MTRSNVLPVA RTYSRTFSGA RLRRLRQERG LTQVALAKAL DLSTSYVNQL ENDQRPITVP
VLLLLTERFD LSAQYFSSDS DARLVADLSD VFTDIGVEHA VSGAQIEEFV ARMPEVGHSL
VAVHRRLRAA TEELEGYRSR ATAETELPPA RPMPFEEVRD FFYDRNNYIH DLDMAAERMF
TESGMRTGGL DIQLAELMRD RFGISVVIDD NLPDTAKRRY HPDTKVLRVA HWLMPGQRAF
QIATQLALVG QSDLISSIVA TDDQLSTEAR GVARIGLANY FAGAFLLPYR EFHRAAEQLR
YDIDLLGRRF GVGFETVCHR LSTLQRPRQR GIPFIFVRTD KAGNISKRQS ATAFHFSRVG
GSCPLWVVHD AFAQPERIVR QVAQMPDGRS YFWVAKTTAA DGLGYLGPHK NFAVGLGCDL
AHAHKLVYST GVVLDDPSTE VPIGAGCKIC NRTSCAQRAF PYLGGRVAVD ENAGSSLPYS
STEQSV
