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Database: UniProt
Entry: A0A229SVN4_9PSEU
LinkDB: A0A229SVN4_9PSEU
Original site: A0A229SVN4_9PSEU 
ID   A0A229SVN4_9PSEU        Unreviewed;       968 AA.
AC   A0A229SVN4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=SARP family transcriptional regulator {ECO:0000313|EMBL:OXM62902.1};
GN   ORFNames=CF165_31450 {ECO:0000313|EMBL:OXM62902.1};
OS   Amycolatopsis vastitatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM62902.1, ECO:0000313|Proteomes:UP000215199};
RN   [1] {ECO:0000313|Proteomes:UP000215199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA   Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA   Kalinowski J., Ziemert N.;
RT   "Comparative genome mining reveals phylogenetic distribution patterns of
RT   secondary metabolites in Amycolatopsis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC       {ECO:0000256|ARBA:ARBA00005820}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXM62902.1}.
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DR   EMBL; NMUL01000038; OXM62902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229SVN4; -.
DR   Proteomes; UP000215199; Unassembled WGS sequence.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0098542; P:defense response to other organism; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15831; BTAD; 1.
DR   Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR042197; Apaf_helical.
DR   InterPro; IPR005158; BTAD.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR35807:SF1; TRANSCRIPTIONAL REGULATOR REDD; 1.
DR   PANTHER; PTHR35807; TRANSCRIPTIONAL REGULATOR REDD-RELATED; 1.
DR   Pfam; PF03704; BTAD; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00028; TPR; 6.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}.
FT   DOMAIN          1..98
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        1..98
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   REGION          622..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   968 AA;  105901 MW;  781BDC8F8F43D88D CRC64;
     MPTRRDMRFR VLGPLEFLDD GEWRRVGAAK WRTLLAVLLA KPDRVVSADR IAVELWGERP
     PKTVDNQIYG YVARLRRLLN ADRDQLLVTH SPGYRLCAGF EDIDAGRFTA LAEQGRAALR
     AGDAGTATRH LDAALALWRG SPFEDVPATP MVQAEADRLT EARAGALEDW AEAQLALGEH
     AEVVSRLADF VPRHPLRERL RELQMLALYR QGRQADALAG YLELRTLLAE ELGVDPGQSI
     RHRYEQIVRA DPALTEAVSR VDPVRQLPPD IPDFAGRAEE LARVSGTVSS GSADGPPSVV
     VLTGAPGVGK SSLAVHAAHA LASRFPDGQL YLDLAGTSPR PQDPAVLLAE MLGAVGVRGE
     WIPDDLRARA ALYRSMLARR RMLIVLDDAD SAGQVRPLLP STGSCAVIIT TRRPISDLSG
     TWHVELDVFE PATARELFTS IVGESRVAAE PEQADAILRA CGNLPLAIRI SGAKLAGRPK
     WPLRVLAERL DDESQRLDEL RVGELGVRAS FELSLRSLPA DAVRGFALLG LFCGPVPSWV
     LGPLLDRAHA DDVMDLLLDA NLVQISGTDE TGQPRYRLPG LLRDYAAETA ATYPLPTRQA
     AVAHLLATWL DLAEHAAGHL PPSLFRPTPG TAPRRPGPTD VRRRAATDPL GWFDAERATV
     LDAVALAADW GLHEAAWELA VAMVPYYDLR SLYQEWLRGH EIALGAVREA GNGRGEAVLL
     KDLAQVQIYR DQFDSATPNL HRSLALYQQA GDRRGEALAT AALATIERVH GRYEHALDQA
     IRALDLVIAT GDQHIEAQLR NGVAGIHLAQ GRTADARAWF DEALALSRKL GDVHREAVVL
     REMSLLHEDS DEALECLQTA HDIFDDLHDE RCVAYTLLRM GRVHAGRRDS ARTAEVLTRA
     AKVFERDGDR LGEASCWQLL GELDIGYADP VAARTHLSRA LQLWQTFGKH EPAVAVAAQL
     QQLQIGRS
//
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