RHAR_SALPK
ID RHAR_SALPK Reviewed; 282 AA.
AC B5BJG9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=HTH-type transcriptional activator RhaR {ECO:0000255|HAMAP-Rule:MF_01533};
DE AltName: Full=L-rhamnose operon transcriptional activator RhaR {ECO:0000255|HAMAP-Rule:MF_01533};
GN Name=rhaR {ECO:0000255|HAMAP-Rule:MF_01533}; OrderedLocusNames=SSPA3620;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
CC -!- FUNCTION: Activates expression of the rhaSR operon in response to L-
CC rhamnose. {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01533}.
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DR EMBL; FM200053; CAR61902.1; -; Genomic_DNA.
DR RefSeq; WP_000013290.1; NC_011147.1.
DR AlphaFoldDB; B5BJG9; -.
DR SMR; B5BJG9; -.
DR KEGG; sek:SSPA3620; -.
DR HOGENOM; CLU_000445_88_5_6; -.
DR OMA; NREVGMT; -.
DR Proteomes; UP000001869; 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_01533; HTH_type_RhaR; 1.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR023699; Tscrpt_act_RhaR.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
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; 1.
DR SUPFAM; SSF51182; SSF51182; 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..282
FT /note="HTH-type transcriptional activator RhaR"
FT /id="PRO_1000200943"
FT DOMAIN 179..277
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT DNA_BIND 196..217
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT DNA_BIND 244..267
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT SITE 246
FT /note="Interaction with sigma-70"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
SQ SEQUENCE 282 AA; 32858 MW; 657BF8FE7DE1CF20 CRC64;
MANQLILLKK DFFTDEQQAV TVADRYPQDV FAEHTHEFCE LVMVWRGNGL HVLNERPYRI
TRGDLFYIRA EDKHSYTSVN DLVLQNIIYC PERLKLNVNW QAMIPGFQGA QWHPHWRLGS
MGMNQARQVI NQLEHESNGR DPLANEMAEL LFGQLVMTLK RHRYATDDLP ATSRETLLDK
LITALANSLE CPFALDAFCQ QEQCSERVLR QQFRAQTGMT INQYLRQVRI CHAQYLLQHS
PLMISEISMQ CGFEDSNYFS VVFTRETGMT PSQWRHLSNQ SD