RHAS_PECCP
ID RHAS_PECCP Reviewed; 279 AA.
AC C6DJR4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=HTH-type transcriptional activator RhaS {ECO:0000255|HAMAP-Rule:MF_01534};
DE AltName: Full=L-rhamnose operon regulatory protein RhaS {ECO:0000255|HAMAP-Rule:MF_01534};
GN Name=rhaS {ECO:0000255|HAMAP-Rule:MF_01534}; OrderedLocusNames=PC1_0421;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates expression of the rhaBAD and rhaT operons.
CC {ECO:0000255|HAMAP-Rule:MF_01534}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000255|HAMAP-Rule:MF_01534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01534}.
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DR EMBL; CP001657; ACT11477.1; -; Genomic_DNA.
DR RefSeq; WP_012773133.1; NC_012917.1.
DR AlphaFoldDB; C6DJR4; -.
DR SMR; C6DJR4; -.
DR STRING; 561230.PC1_0421; -.
DR EnsemblBacteria; ACT11477; ACT11477; PC1_0421.
DR KEGG; pct:PC1_0421; -.
DR eggNOG; COG1917; Bacteria.
DR eggNOG; COG2169; Bacteria.
DR HOGENOM; CLU_000445_88_5_6; -.
DR OMA; GHYPSHW; -.
DR OrthoDB; 1268974at2; -.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01534; HTH_type_RhaS; 1.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR037923; HTH-like.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR InterPro; IPR023609; Tscrpt_reg_HTH_RhaS.
DR Pfam; PF02311; AraC_binding; 1.
DR Pfam; PF12833; HTH_18; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF51215; SSF51215; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Repeat; Rhamnose metabolism;
KW Transcription; Transcription regulation.
FT CHAIN 1..279
FT /note="HTH-type transcriptional activator RhaS"
FT /id="PRO_1000215405"
FT DOMAIN 175..273
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT DNA_BIND 192..213
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT DNA_BIND 240..263
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT SITE 251
FT /note="Interaction with sigma-70"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
SQ SEQUENCE 279 AA; 31839 MW; 45FE5140B054A5A1 CRC64;
MTLLRGDDFF TSRAVTVAVE PRTPQTAFPE HYHDFWEIVL VEQGAGVHVF NDQPYALCSG
SVFFVRDNDR HLFEDVEGLC LTNMLYRSPR GFRFLSDIAA FLPYGPNGEW QGQWQVNAAG
MQQLKQSLNS LAELAQSDAP EAIAASESLF LHILVQLRQQ CFQTQSSGSE RQGVQALLGW
LQNNYSEEVN WGSLADRFSL PLRTLHRQLK QHTGMTPQRY LNRLRLLEAR RRLQQSDDSI
TTIAHACGFS DSNHFSTQFR KAFSQAPKSL RHQAFSREE