KSTR2_MYCTU
ID KSTR2_MYCTU Reviewed; 200 AA.
AC P9WMB9; L0TD56; P96839; Q7D5A5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=HTH-type transcriptional repressor KstR2;
GN Name=kstR2; OrderedLocusNames=Rv3557c;
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 REGULATOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20167624; DOI=10.1099/mic.0.034538-0;
RA Kendall S.L., Burgess P., Balhana R., Withers M., Ten Bokum A., Lott J.S.,
RA Gao C., Uhia-Castro I., Stoker N.G.;
RT "Cholesterol utilization in mycobacteria is controlled by two TetR-type
RT transcriptional regulators: kstR and kstR2.";
RL Microbiology 156:1362-1371(2010).
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 a small regulon that may play a
CC role in the utilization of cholesterol. {ECO:0000269|PubMed:20167624}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AL123456; CCP46379.1; -; Genomic_DNA.
DR PIR; C70604; C70604.
DR RefSeq; NP_218074.1; NC_000962.3.
DR RefSeq; WP_003419329.1; NZ_NVQJ01000014.1.
DR PDB; 4W1U; X-ray; 1.88 A; A=1-200.
DR PDB; 4W97; X-ray; 1.60 A; A=2-200.
DR PDBsum; 4W1U; -.
DR PDBsum; 4W97; -.
DR AlphaFoldDB; P9WMB9; -.
DR SMR; P9WMB9; -.
DR STRING; 83332.Rv3557c; -.
DR PaxDb; P9WMB9; -.
DR DNASU; 887467; -.
DR GeneID; 45427541; -.
DR GeneID; 887467; -.
DR KEGG; mtu:Rv3557c; -.
DR TubercuList; Rv3557c; -.
DR eggNOG; COG1309; Bacteria.
DR OMA; ARQYLSM; -.
DR PhylomeDB; P9WMB9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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; IPR041490; KstR2_TetR_C.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR Pfam; PF17932; TetR_C_24; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 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..200
FT /note="HTH-type transcriptional repressor KstR2"
FT /id="PRO_0000405031"
FT DOMAIN 9..69
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 32..51
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:4W97"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:4W1U"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:4W97"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 54..79
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 123..144
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:4W97"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4W97"
FT HELIX 180..195
FT /evidence="ECO:0007829|PDB:4W97"
SQ SEQUENCE 200 AA; 22906 MW; E1B29D39CF4D955F CRC64;
MDRVAGQVNS RRGELLELAA AMFAERGLRA TTVRDIADGA GILSGSLYHH FASKEEMVDE
LLRGFLDWLF ARYRDIVDST ANPLERLQGL FMASFEAIEH HHAQVVIYQD EAQRLASQPR
FSYIEDRNKQ QRKMWVDVLN QGIEEGYFRP DLDVDLVYRF IRDTTWVSVR WYRPGGPLTA
QQVGQQYLAI VLGGITKEGV
