ID   MTRR_NEIGO              Reviewed;         210 AA.
AC   P39897;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=HTH-type transcriptional regulator MtrR {ECO:0000305};
DE   AltName: Full=Multiple transferrable resistance regulator {ECO:0000303|PubMed:9209024};
GN   Name=mtrR {ECO:0000303|PubMed:8196548};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=FA19;
RX   PubMed=8196548; DOI=10.1111/j.1365-2958.1994.tb00354.x;
RA   Pan W., Spratt B.G.;
RT   "Regulation of the permeability of the gonococcal cell envelope by the mtr
RT   system.";
RL   Mol. Microbiol. 11:769-775(1994).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF GLY-45.
RC   STRAIN=FA19;
RX   PubMed=9209024; DOI=10.1128/jb.179.13.4123-4128.1997;
RA   Lucas C.E., Balthazar J.T., Hagman K.E., Shafer W.M.;
RT   "The MtrR repressor binds the DNA sequence between the mtrR and mtrC genes
RT   of Neisseria gonorrhoeae.";
RL   J. Bacteriol. 179:4123-4128(1997).
RN   [3]
RP   FUNCTION.
RC   STRAIN=FA19;
RX   PubMed=14645274; DOI=10.1128/jb.185.24.7145-7152.2003;
RA   Lee E.H., Rouquette-Loughlin C., Folster J.P., Shafer W.M.;
RT   "FarR regulates the farAB-encoded efflux pump of Neisseria gonorrhoeae via
RT   an MtrR regulatory mechanism.";
RL   J. Bacteriol. 185:7145-7152(2003).
RN   [4]
RP   DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RC   STRAIN=FA19;
RX   PubMed=15995218; DOI=10.1128/jb.187.14.5008-5012.2005;
RA   Hoffmann K.M., Williams D., Shafer W.M., Brennan R.G.;
RT   "Characterization of the multiple transferable resistance repressor, MtrR,
RT   from Neisseria gonorrhoeae.";
RL   J. Bacteriol. 187:5008-5012(2005).
RN   [5]
RP   FUNCTION, AND DNA-BINDING.
RC   STRAIN=FA19;
RX   PubMed=23221802; DOI=10.1128/mbio.00446-12;
RA   Zalucki Y.M., Dhulipala V., Shafer W.M.;
RT   "Dueling regulatory properties of a transcriptional activator (MtrA) and
RT   repressor (MtrR) that control efflux pump gene expression in Neisseria
RT   gonorrhoeae.";
RL   MBio 3:E00446-E00446(2012).
RN   [6] {ECO:0007744|PDB:3VIB}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RA   Kumaraswami M., Shafer W.M., Brennan R.G.;
RT   "Structural basis for multidrug recognitionand antimicrobial resistance by
RT   MtrR, an efflux pump regulator from Neisseria gonorrhoeae.";
RL   Submitted (SEP-2011) to the PDB data bank.
CC   -!- FUNCTION: Controls the permeability of the cell envelope to hydrophobic
CC       compounds such as antibiotics and detergents (PubMed:8196548).
CC       Represses transcription of the mtrCDE-encoded efflux pump by binding
CC       within the mtrCDE promoter (PubMed:9209024, PubMed:23221802). Also
CC       negatively regulates the expression of farR, by binding to its promoter
CC       region, leading indirectly to the positive regulation of expression of
CC       the farAB-encoded efflux pump (PubMed:14645274).
CC       {ECO:0000269|PubMed:14645274, ECO:0000269|PubMed:23221802,
CC       ECO:0000269|PubMed:8196548, ECO:0000269|PubMed:9209024}.
CC   -!- ACTIVITY REGULATION: DNA binding is affected significantly by
CC       increasing the NaCl concentration. {ECO:0000269|PubMed:15995218}.
CC   -!- SUBUNIT: Homodimer. Binds to DNA as a pair of dimers.
CC       {ECO:0000269|PubMed:15995218}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene results in increased
CC       resistance to antibiotics and detergents. {ECO:0000269|PubMed:8196548}.
CC   -!- MISCELLANEOUS: The MtrA and MtrR-binding sites are sterically close and
CC       addition of an effector increases the affinity of MtrA for the mtrCDE
CC       promoter such that MtrR binding is negatively impacted.
CC       {ECO:0000305|PubMed:23221802}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z25797; CAA81047.1; -; Genomic_DNA.
DR   PIR; S42419; S42419.
DR   RefSeq; WP_003693763.1; NZ_WHPJ01000003.1.
DR   PDB; 3VIB; X-ray; 2.40 A; A/B/C/D=1-210.
DR   PDB; 6OF0; X-ray; 2.00 A; A/B/C/D=1-210.
DR   PDB; 7JNP; X-ray; 2.60 A; A/B=1-210.
DR   PDB; 7JU3; X-ray; 2.70 A; A/B=1-210.
DR   PDBsum; 3VIB; -.
DR   PDBsum; 6OF0; -.
DR   PDBsum; 7JNP; -.
DR   PDBsum; 7JU3; -.
DR   AlphaFoldDB; P39897; -.
DR   SMR; P39897; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   InterPro; IPR013572; Tscrpt_reg_MAATS_C.
DR   Pfam; PF08361; TetR_C_2; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00455; HTHTETR.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF48498; SSF48498; 1.
DR   PROSITE; PS01081; HTH_TETR_1; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..210
FT                   /note="HTH-type transcriptional regulator MtrR"
FT                   /id="PRO_0000070606"
FT   DOMAIN          9..69
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   DNA_BIND        32..51
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   VARIANT         105
FT                   /note="H -> Y (in penicillin-resistant isolates)"
FT   MUTAGEN         45
FT                   /note="G->D: Does not bind DNA."
FT                   /evidence="ECO:0000269|PubMed:9209024"
FT   HELIX           9..26
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:3VIB"
FT   HELIX           33..40
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           54..70
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           84..101
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           123..149
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           159..179
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           186..203
FT                   /evidence="ECO:0007829|PDB:6OF0"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:6OF0"
SQ   SEQUENCE   210 AA;  24193 MW;  41E26446CBEF57F2 CRC64;
     MRKTKTEALK TKEHLMLAAL ETFYRKGIAR TSLNEIAQAA GVTRGALYWH FKNKEDLFDA
     LFQRICDDIE NCIAQDAADA EGGSWTVFRH TLLHFFERLQ SNDIHYKFHN ILFLKCEHTE
     QNAAVIAIAR KHQAIWREKI TAVLTEAVEN QDLADDLDKE TAVIFIKSTL DGLIWRWFSS
     GESFDLGKTA PRIIGIMMDN LENHPCLRRK