KSTR_MYCTU
ID KSTR_MYCTU Reviewed; 220 AA.
AC P96856; L0TEJ7;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 5.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=HTH-type transcriptional repressor KstR;
GN Name=kstR; OrderedLocusNames=Rv3574;
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 AS A TRANSCRIPTIONAL REPRESSOR, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17635188; DOI=10.1111/j.1365-2958.2007.05827.x;
RA Kendall S.L., Withers M., Soffair C.N., Moreland N.J., Gurcha S.,
RA Sidders B., Frita R., Ten Bokum A., Besra G.S., Lott J.S., Stoker N.G.;
RT "A highly conserved transcriptional repressor controls a large regulon
RT involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium
RT tuberculosis.";
RL Mol. Microbiol. 65:684-699(2007).
RN [3]
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).
CC -!- FUNCTION: Controls the expression of genes used for utilizing diverse
CC lipids as energy sources. {ECO:0000269|PubMed:17635188}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17635188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46397.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
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DR EMBL; AL123456; CCP46397.1; ALT_INIT; Genomic_DNA.
DR PIR; D70606; D70606.
DR RefSeq; NP_218091.3; NC_000962.3.
DR PDB; 3MNL; X-ray; 1.80 A; A/B=22-220.
DR PDB; 5AQC; X-ray; 1.66 A; A/B=23-220.
DR PDB; 5CW8; X-ray; 2.60 A; A/B=22-220.
DR PDB; 5CXG; X-ray; 2.10 A; A/B/C/D=20-220.
DR PDB; 5CXI; X-ray; 2.00 A; A/B=22-220.
DR PDB; 5FMP; X-ray; 2.26 A; A/B=23-220.
DR PDB; 5UA1; X-ray; 2.90 A; A/B=20-220.
DR PDB; 5UA2; X-ray; 2.90 A; A=1-220.
DR PDBsum; 3MNL; -.
DR PDBsum; 5AQC; -.
DR PDBsum; 5CW8; -.
DR PDBsum; 5CXG; -.
DR PDBsum; 5CXI; -.
DR PDBsum; 5FMP; -.
DR PDBsum; 5UA1; -.
DR PDBsum; 5UA2; -.
DR AlphaFoldDB; P96856; -.
DR SMR; P96856; -.
DR STRING; 83332.Rv3574; -.
DR PaxDb; P96856; -.
DR DNASU; 887204; -.
DR GeneID; 887204; -.
DR KEGG; mtu:Rv3574; -.
DR TubercuList; Rv3574; -.
DR eggNOG; COG1309; Bacteria.
DR InParanoid; P96856; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR041642; KstR_C.
DR Pfam; PF17925; TetR_C_20; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..220
FT /note="HTH-type transcriptional repressor KstR"
FT /id="PRO_0000405028"
FT DOMAIN 36..96
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 59..78
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT HELIX 34..57
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5AQC"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5FMP"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:5AQC"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 172..193
FT /evidence="ECO:0007829|PDB:5AQC"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:5AQC"
SQ SEQUENCE 220 AA; 24050 MW; 085E69F84C6982C6 CRC64;
MSSANTNTSS APDAPPRAVM KVAVLAESEL GSEAQRERRK RILDATMAIA SKGGYEAVQM
RAVADRADVA VGTLYRYFPS KVHLLVSALG REFSRIDAKT DRSAVAGATP FQRLNFMVGK
LNRAMQRNPL LTEAMTRAYV FADASAASEV DQVEKLIDSM FARAMANGEP TEDQYHIARV
ISDVWLSNLL AWLTRRASAT DVSKRLDLAV RLLIGDQDSA
