RIPA_CORGL
ID RIPA_CORGL Reviewed; 331 AA.
AC Q8NRR3; Q5QHF9; Q6M6H3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=HTH-type transcriptional regulator RipA {ECO:0000303|PubMed:16179344};
DE AltName: Full=AraC-type regulator RipA {ECO:0000303|PubMed:16179344};
DE AltName: Full=Repressor of iron proteins A {ECO:0000303|PubMed:16179344};
DE Short=RIPA {ECO:0000303|PubMed:16179344};
GN Name=ripA {ECO:0000303|PubMed:16179344}; OrderedLocusNames=Cgl0982, cg1120;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Park S.-D., Park I.-H., Lee S.-N., Lee H.-S.;
RT "Corynebacterium glutamicum isolate promoter functional region.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16179344; DOI=10.1074/jbc.m508693200;
RA Wennerhold J., Krug A., Bott M.;
RT "The AraC-type regulator RipA represses aconitase and other iron proteins
RT from Corynebacterium under iron limitation and is itself repressed by
RT DtxR.";
RL J. Biol. Chem. 280:40500-40508(2005).
CC -!- FUNCTION: Under iron limitation, RipA negatively controls the
CC expression of the acn (aconitase), catA (catechol 1,2 dioxygenase),
CC leuCD (isopropylmalate dehydratase), narKGHJI (nitrite/nitrate
CC transporter and nitrate reductase), sdhCAB (succinate dehydrogenase),
CC pta (phosphotransacetylase) and katA (catalase) genes. Binds to the
CC consensus sequence in the promoter region.
CC {ECO:0000269|PubMed:16179344}.
CC -!- INDUCTION: Repressed by DtxR under iron excess.
CC {ECO:0000269|PubMed:16179344}.
CC -!- DISRUPTION PHENOTYPE: Under iron limitation, the ripA deletion mutant
CC shows a 2-fold higher aconitase activity and a higher mRNA level for
CC the acn, catA, leuCD, narKGHJI, sdhCAB and pta genes.
CC {ECO:0000269|PubMed:16179344}.
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DR EMBL; BA000036; BAB98375.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19689.1; -; Genomic_DNA.
DR EMBL; AY513595; AAS92713.1; -; Genomic_DNA.
DR RefSeq; NP_600210.1; NC_003450.3.
DR RefSeq; WP_011014026.1; NC_006958.1.
DR AlphaFoldDB; Q8NRR3; -.
DR SMR; Q8NRR3; -.
DR STRING; 196627.cg1120; -.
DR DNASU; 1018972; -.
DR KEGG; cgb:cg1120; -.
DR KEGG; cgl:Cgl0982; -.
DR PATRIC; fig|196627.13.peg.966; -.
DR eggNOG; COG2207; Bacteria.
DR HOGENOM; CLU_810658_0_0_11; -.
DR OMA; HPSECIA; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF12833; HTH_18; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..331
FT /note="HTH-type transcriptional regulator RipA"
FT /id="PRO_0000223239"
FT DOMAIN 112..209
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 129..150
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 176..199
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT CONFLICT 16..28
FT /note="VRFGERIFTLVAG -> SSVLAREFSLSSQA (in Ref. 3;
FT AAS92713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36045 MW; 0F3449B8CFED20DA CRC64;
MSSASLLWCH SGVSTVRFGE RIFTLVAGDL LFAPEEAQVA DDSQGLVLNI RFETLNIMGP
ARRIHLGHVW NDRLTFEYSR SLFGKETLSP DIARLFTDRV PTPPLPAPRK ARAVAQVLVS
NPADQTSLEE FAEIQGVSAR TLQRQFLKST GYSFSEWRAA QRVCVAASLL AHDFSISVVA
NLVGFAATSS LTRAFRRHTG ATPSTFTTGQ IGMGSAGHPP RIPATTTFAE AHQDQQLWIY
SGTATVTTPG YCRFMGQGDM VTIPAGTQTR IDVAAGSIAF PVPVGLDEWG MDLTRVVAVN
NQQPKPLTIL EQSEWSKLSE ELLNTPVPVQ M
