ID   TIPA_STRLI              Reviewed;         253 AA.
AC   P0A4T9; P32184;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=HTH-type transcriptional activator TipA;
GN   Name=tipA;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2537819; DOI=10.1128/jb.171.3.1459-1466.1989;
RA   Murakami T., Holt T.G., Thompson C.J.;
RT   "Thiostrepton-induced gene expression in Streptomyces lividans.";
RL   J. Bacteriol. 171:1459-1466(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RX   PubMed=7688297; DOI=10.1002/j.1460-2075.1993.tb05987.x;
RA   Holmes D.J., Caso J.L., Thompson C.J.;
RT   "Autogenous transcriptional activation of a thiostrepton-induced gene in
RT   Streptomyces lividans.";
RL   EMBO J. 12:3183-3191(1993).
CC   -!- FUNCTION: Transcriptional activator. Is activated when bound to the
CC       antibiotic thiostrepton.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long; Synonyms=TipA-L;
CC         IsoId=P0A4T9-1; Sequence=Displayed;
CC       Name=Short; Synonyms=TipA-S;
CC         IsoId=P0A4T9-2; Sequence=VSP_018752;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC13653.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; S64314; AAB27737.1; -; Genomic_DNA.
DR   EMBL; M24524; AAC13653.1; ALT_INIT; Genomic_DNA.
DR   PIR; S35354; S35354.
DR   PDB; 1NY9; NMR; -; A=111-253.
DR   PDB; 2MBZ; NMR; -; A=110-253.
DR   PDB; 2MC0; NMR; -; A=110-253.
DR   PDB; 2VZ4; X-ray; 2.90 A; A=2-109.
DR   PDBsum; 1NY9; -.
DR   PDBsum; 2MBZ; -.
DR   PDBsum; 2MC0; -.
DR   PDBsum; 2VZ4; -.
DR   AlphaFoldDB; P0A4T9; -.
DR   BMRB; P0A4T9; -.
DR   SMR; P0A4T9; -.
DR   EvolutionaryTrace; P0A4T9; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   DisProt; DP00997; -.
DR   Gene3D; 1.10.490.50; -; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   InterPro; IPR036244; TipA-like_antibiotic-bd.
DR   InterPro; IPR012925; TipAS_dom.
DR   Pfam; PF13411; MerR_1; 1.
DR   Pfam; PF07739; TipAS; 1.
DR   PRINTS; PR00040; HTHMERR.
DR   SMART; SM00422; HTH_MERR; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF89082; SSF89082; 1.
DR   PROSITE; PS00552; HTH_MERR_1; 1.
DR   PROSITE; PS50937; HTH_MERR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative initiation; Direct protein sequencing;
KW   DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..253
FT                   /note="HTH-type transcriptional activator TipA"
FT                   /id="PRO_0000013606"
FT   DOMAIN          1..71
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   DNA_BIND        5..24
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   VAR_SEQ         1..109
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018752"
FT   HELIX           5..12
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   HELIX           16..24
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   HELIX           43..57
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   HELIX           62..69
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   HELIX           79..105
FT                   /evidence="ECO:0007829|PDB:2VZ4"
FT   HELIX           116..123
FT                   /evidence="ECO:0007829|PDB:2MBZ"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:2MBZ"
FT   HELIX           132..138
FT                   /evidence="ECO:0007829|PDB:2MBZ"
FT   HELIX           144..152
FT                   /evidence="ECO:0007829|PDB:2MBZ"
FT   HELIX           165..180
FT                   /evidence="ECO:0007829|PDB:1NY9"
FT   HELIX           187..203
FT                   /evidence="ECO:0007829|PDB:1NY9"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:1NY9"
FT   HELIX           223..229
FT                   /evidence="ECO:0007829|PDB:1NY9"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:1NY9"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:2MC0"
FT   HELIX           236..251
FT                   /evidence="ECO:0007829|PDB:1NY9"
SQ   SEQUENCE   253 AA;  28711 MW;  0B32F6191BF2B779 CRC64;
     MSYSVGQVAG FAGVTVRTLH HYDDIGLLVP SERSHAGHRR YSDADLDRLQ QILFYRELGF
     PLDEVAALLD DPAADPRAHL RRQHELLSAR IGKLQKMAAA VEQAMEARSM GINLTPEEKF
     EVFGDFDPDQ YEEEVRERWG NTDAYRQSKE KTASYTKEDW QRIQDEADEL TRRFVALMDA
     GEPADSEGAM DAAEDHRQGI ARNHYDCGYE MHTCLGEMYV SDERFTRNID AAKPGLAAYM
     RDAILANAVR HTP