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RICR_MYCTU
ID   RICR_MYCTU              Reviewed;          96 AA.
AC   O07434; D9CH46; F2GLY8; Q7DAA9;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Copper-sensing transcriptional repressor RicR {ECO:0000305};
DE   AltName: Full=Regulated in copper repressor {ECO:0000303|PubMed:21166899};
GN   Name=ricR {ECO:0000303|PubMed:21166899};
GN   OrderedLocusNames=Rv0190 {ECO:0000312|EMBL:CCP42917.1},
GN   RVBD_0190 {ECO:0000312|EMBL:AFN48039.1};
GN   ORFNames=LH57_01055 {ECO:0000312|EMBL:AIR12914.1},
GN   P425_00198 {ECO:0000312|EMBL:KBJ41298.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A REPRESSOR, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21166899; DOI=10.1111/j.1365-2958.2010.07431.x;
RA   Festa R.A., Jones M.B., Butler-Wu S., Sinsimer D., Gerads R., Bishai W.R.,
RA   Peterson S.N., Darwin K.H.;
RT   "A novel copper-responsive regulon in Mycobacterium tuberculosis.";
RL   Mol. Microbiol. 79:133-148(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genome Sequencing Platform;
RA   Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA   Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA   Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF CYS-38.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=24549843; DOI=10.1128/mbio.00876-13;
RA   Shi X., Festa R.A., Ioerger T.R., Butler-Wu S., Sacchettini J.C.,
RA   Darwin K.H., Samanovic M.I.;
RT   "The copper-responsive RicR regulon contributes to Mycobacterium
RT   tuberculosis virulence.";
RL   MBio 5:E00876-E00876(2014).
CC   -!- FUNCTION: Under low copper conditions, represses the expression of
CC       lpqS, Rv2963, mymT, socA, socB, mmcO and its own expression. In the
CC       presence of copper, RicR dissociates from DNA, leading to the
CC       expression of the target genes. Members of the RicR regulon are
CC       important for copper resistance during infections and full virulence in
CC       a mouse model of infection. {ECO:0000269|PubMed:21166899,
CC       ECO:0000269|PubMed:24549843}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Negatively autoregulated. Induced by copper.
CC       {ECO:0000269|PubMed:21166899}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene results in the
CC       constitutive expression of the entire RicR regulon and hyper-resistance
CC       of the cell to copper. {ECO:0000269|PubMed:21166899}.
CC   -!- MISCELLANEOUS: Constitutive repression of the RicR regulon by a
CC       'copper-blind' RicR results in extreme copper sensitivity in vitro and
CC       attenuation of virulence in mice. {ECO:0000269|PubMed:24549843}.
CC   -!- SIMILARITY: Belongs to the CsoR family. {ECO:0000305}.
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DR   EMBL; GU726749; ADJ67803.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP42917.1; -; Genomic_DNA.
DR   EMBL; CP003248; AFN48039.1; -; Genomic_DNA.
DR   EMBL; JLDD01000001; KBJ41298.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR12914.1; -; Genomic_DNA.
DR   RefSeq; NP_214704.1; NC_000962.3.
DR   RefSeq; WP_003401147.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; O07434; -.
DR   SMR; O07434; -.
DR   STRING; 83332.Rv0190; -.
DR   iPTMnet; O07434; -.
DR   PaxDb; O07434; -.
DR   PRIDE; O07434; -.
DR   DNASU; 886772; -.
DR   GeneID; 45424161; -.
DR   GeneID; 886772; -.
DR   KEGG; mtu:Rv0190; -.
DR   KEGG; mtv:RVBD_0190; -.
DR   PATRIC; fig|83332.111.peg.218; -.
DR   TubercuList; Rv0190; -.
DR   eggNOG; COG1937; Bacteria.
DR   HOGENOM; CLU_130332_0_1_11; -.
DR   OMA; EHLTECI; -.
DR   PhylomeDB; O07434; -.
DR   PHI-base; PHI:4070; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
DR   GO; GO:0046688; P:response to copper ion; IDA:MTBBASE.
DR   Gene3D; 1.20.58.1000; -; 1.
DR   InterPro; IPR003735; Metal_Tscrpt_repr.
DR   InterPro; IPR038390; Metal_Tscrpt_repr_sf.
DR   PANTHER; PTHR33677; PTHR33677; 1.
DR   Pfam; PF02583; Trns_repr_metal; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Copper; Cytoplasm; DNA-binding; Metal-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..96
FT                   /note="Copper-sensing transcriptional repressor RicR"
FT                   /id="PRO_0000433099"
FT   BINDING         38
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP49,
FT                   ECO:0000305|PubMed:24549843"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP49"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP49"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   MUTAGEN         38
FT                   /note="C->A: Unresponsive to copper."
FT                   /evidence="ECO:0000269|PubMed:24549843"
SQ   SEQUENCE   96 AA;  10365 MW;  C7C49AC65C10924E CRC64;
     MTAAHGYTQQ KDNYAKRLRR VEGQVRGIAR MIEEDKYCID VLTQISAVTS ALRSVALNLL
     DEHLSHCVTR AVAEGGPGAD GKLAEASAAI ARLVRS
 
 
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