KSTR2_RHOJR
ID KSTR2_RHOJR Reviewed; 204 AA.
AC Q0S7V2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=HTH-type transcriptional repressor KstR2;
GN Name=kstR2; OrderedLocusNames=RHA1_ro04598;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND SUBUNIT.
RC STRAIN=RHA1;
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of probable transcriptional regulatory protein
RT rha5900.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Controls the expression of a small regulon that may play a
CC role in the utilization of cholesterol. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
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DR EMBL; CP000431; ABG96384.1; -; Genomic_DNA.
DR RefSeq; WP_009477673.1; NC_008268.1.
DR PDB; 2IBD; X-ray; 1.50 A; A/B=1-204.
DR PDBsum; 2IBD; -.
DR AlphaFoldDB; Q0S7V2; -.
DR SMR; Q0S7V2; -.
DR STRING; 101510.RHA1_ro04598; -.
DR EnsemblBacteria; ABG96384; ABG96384; RHA1_ro04598.
DR KEGG; rha:RHA1_ro04598; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_12_4_11; -.
DR OMA; ARQYLSM; -.
DR EvolutionaryTrace; Q0S7V2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS: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..204
FT /note="HTH-type transcriptional repressor KstR2"
FT /id="PRO_0000405033"
FT DOMAIN 13..73
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 36..55
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 58..82
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 126..148
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2IBD"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2IBD"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:2IBD"
SQ SEQUENCE 204 AA; 22550 MW; 6C9FD9985640EEFA CRC64;
MTPPPADDTS GKSGRRTELL DIAATLFAER GLRATTVRDI ADAAGILSGS LYHHFDSKES
MVDEILRGFL DDLFGKYREI VASGLDSRAT LEALVTTSYE AIDASHSAVA IYQDEVKHLV
ANERFTYLSE LNTEFRELWM GVLEAGVKDG SFRSDIDVEL AFRFLRDTAW VAVRWYRPGG
SVTVDTVAKQ YLSIVLDGLA SPHN