Legends: 1, MUTAGEN C->A: Abolishes transcriptional activation. {ECO:0000269|PubMed:2551364}; 2, MUTAGEN C->A: Slight increase in transcriptional activation. {ECO:0000269|PubMed:2551364}; 3, MUTAGEN C->A: Decrease in transcriptional activation. {ECO:0000269|PubMed:2551364}; 4, MUTAGEN C->S: Abolishes transcriptional activation; loss of Hg binding. {ECO:0000269|PubMed:2551364}; 5, HTH merR-type. {ECO:0000255|PROSITE- ProRule:PRU00254}; 6, DNA_BIND H-T-H motif. {ECO:0000255|PROSITE- ProRule:PRU00254}; 7, ipat:HTH_MERR_1 [T]; 8, HELIX {ECO:0000244|PDB:5CRL}; 9, TURN {ECO:0000244|PDB:5CRL}.
|
ID MERR_PSEAI Reviewed; 144 AA.
AC P0A183; P06688;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 18-JAN-2017, entry version 57.
DE RecName: Full=Mercuric resistance operon regulatory protein;
GN Name=merR;
OS Pseudomonas aeruginosa.
OG Plasmid pVS1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn501;
RX PubMed=6091128; DOI=10.1073/pnas.81.19.5975;
RA Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M.,
RA Haberstroh L., Silver S.;
RT "Mercuric ion-resistance operons of plasmid R100 and transposon Tn501:
RT the beginning of the operon including the regulatory region and the
RT first two structural genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984).
RN [2]
RP MUTAGENESIS.
RX PubMed=2551364; DOI=10.1021/bi00441a002;
RA Shewchuk L.M., Verdine G.L., Nash H., Walsh C.T.;
RT "Mutagenesis of the cysteines in the metalloregulatory protein MerR
RT indicates that a metal-bridged dimer activates transcription.";
RL Biochemistry 28:6140-6145(1989).
CC -!- FUNCTION: Mediates the mercuric-dependent induction of mercury
CC resistance operon. In the absence of mercury MerR represses
CC transcription by binding tightly to the mer operator region; when
CC mercury is present the dimeric complex binds a single ion and
CC becomes a potent transcriptional activator, while remaining bound
CC to the mer site.
CC -!- SIMILARITY: Contains 1 HTH merR-type DNA-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00254}.
DR EMBL; Z00027; CAA77320.1; -; Genomic_DNA.
DR PIR; A47593; A47593.
DR RefSeq; WP_003131969.1; NZ_MKEL01000364.1.
DR PDB; 5CRL; X-ray; 2.80 A; A/B=1-134.
DR PDBsum; 5CRL; -.
DR ProteinModelPortal; P0A183; -.
DR SMR; P0A183; -.
DR GeneID; 29509533; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045340; F:mercury ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR CDD; cd04783; HTH_MerR1; 1.
DR InterPro; IPR009061; DNA-bd_dom_put.
DR InterPro; IPR011794; MerR.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR Pfam; PF00376; MerR; 1.
DR Pfam; PF09278; MerR-DNA-bind; 1.
DR PRINTS; PR00040; HTHMERR.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR02051; MerR; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Mercuric resistance; Mercury;
KW Metal-binding; Plasmid; Repressor; Transcription;
KW Transcription regulation; Transposable element.
FT CHAIN 1 144 Mercuric resistance operon regulatory
FT protein.
FT /FTId=PRO_0000098136.
FT DOMAIN 7 76 HTH merR-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00254}.
FT DNA_BIND 10 29 H-T-H motif. {ECO:0000255|PROSITE-
FT ProRule:PRU00254}.
FT METAL 82 82 Mercury.
FT METAL 117 117 Mercury.
FT METAL 126 126 Mercury.
FT MUTAGEN 82 82 C->A: Abolishes transcriptional
FT activation. {ECO:0000269|PubMed:2551364}.
FT MUTAGEN 115 115 C->A: Slight increase in transcriptional
FT activation. {ECO:0000269|PubMed:2551364}.
FT MUTAGEN 117 117 C->A: Decrease in transcriptional
FT activation. {ECO:0000269|PubMed:2551364}.
FT MUTAGEN 126 126 C->S: Abolishes transcriptional
FT activation; loss of Hg binding.
FT {ECO:0000269|PubMed:2551364}.
FT HELIX 10 17 {ECO:0000244|PDB:5CRL}.
FT HELIX 21 29 {ECO:0000244|PDB:5CRL}.
FT HELIX 48 62 {ECO:0000244|PDB:5CRL}.
FT HELIX 67 75 {ECO:0000244|PDB:5CRL}.
FT TURN 76 78 {ECO:0000244|PDB:5CRL}.
FT HELIX 82 118 {ECO:0000244|PDB:5CRL}.
FT HELIX 127 132 {ECO:0000244|PDB:5CRL}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 8 77 ismart:HTH_MERR [T]
FT MYHIT 11 33 ipat:HTH_MERR_1 [T]
FT MYHIT 9 46 ipfam:MerR [T]
FT MYHIT 51 113 ipfam:MerR-DNA-bind [T]
FT MYHIT 7 76 iprf:HTH_MERR_2 [T]
SQ SEQUENCE 144 AA; 15763 MW; C573298AFF0846EF CRC64;
MENNLENLTI GVFAKAAGVN VETIRFYQRK GLLLEPDKPY GSIRRYGEAD VTRVRFVKSA
QRLGFSLDEI AELLRLEDGT HCEEASSLAE HKLKDVREKM ADLARMEAVL SELVCACHAR
RGNVSCPLIA SLQGGASLAG SAMP
//
|
