ID   MTRA_NEIGO              Reviewed;         301 AA.
AC   Q9WW32;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=HTH-type transcriptional regulator MtrA {ECO:0000305};
DE   AltName: Full=Mtr activator {ECO:0000303|PubMed:10417654};
GN   Name=mtrA {ECO:0000303|PubMed:10417654};
GN   ORFNames=NCTC10931_01062 {ECO:0000312|EMBL:SUA05978.1};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=FA19 {ECO:0000312|EMBL:AAD44693.1},
RC   FA889 {ECO:0000312|EMBL:AAD44694.1}, and UU1 {ECO:0000312|EMBL:AAD44695.1};
RX   PubMed=10417654; DOI=10.1046/j.1365-2958.1999.01517.x;
RA   Rouquette C., Harmon J.B., Shafer W.M.;
RT   "Induction of the mtrCDE-encoded efflux pump system of Neisseria
RT   gonorrhoeae requires MtrA, an AraC-like protein.";
RL   Mol. Microbiol. 33:651-658(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10931;
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND MUTAGENESIS OF ALA-227;
RP   ARG-231 AND LYS-281.
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).
CC   -!- FUNCTION: Involved in the induction of the mtrCDE-encoded efflux pump
CC       (PubMed:10417654). Binds specifically to the mtrCDE promoter region
CC       (PubMed:23221802). Required for high-level inducible resistance to the
CC       detergent Triton X-100 (TX-100) and the spermicide nonoxynol-9 (N-9)
CC       (PubMed:10417654). {ECO:0000269|PubMed:10417654,
CC       ECO:0000269|PubMed:23221802}.
CC   -!- ACTIVITY REGULATION: The affinity for the mtrCDE promoter increases 2-
CC       fold in the presence of TX-100, a known effector and substrate of the
CC       MtrCDE pump. {ECO:0000269|PubMed:23221802}.
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}.
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DR   EMBL; AF128627; AAD44693.1; -; Genomic_DNA.
DR   EMBL; AF128628; AAD44694.1; -; Genomic_DNA.
DR   EMBL; AF128629; AAD44695.1; -; Genomic_DNA.
DR   EMBL; UGRK01000002; SUA05978.1; -; Genomic_DNA.
DR   RefSeq; WP_003689713.1; NZ_VAHL01000012.1.
DR   AlphaFoldDB; Q9WW32; -.
DR   SMR; Q9WW32; -.
DR   GeneID; 66752464; -.
DR   PATRIC; fig|485.43.peg.1137; -.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR032783; AraC_lig.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF12852; Cupin_6; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..301
FT                   /note="HTH-type transcriptional regulator MtrA"
FT                   /id="PRO_0000445986"
FT   DOMAIN          196..297
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        216..237
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        264..287
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   MUTAGEN         227
FT                   /note="A->L: Decreases DNA binding."
FT                   /evidence="ECO:0000269|PubMed:23221802"
FT   MUTAGEN         231
FT                   /note="R->L: Decreases DNA binding."
FT                   /evidence="ECO:0000269|PubMed:23221802"
FT   MUTAGEN         281
FT                   /note="K->L: Decreases DNA binding."
FT                   /evidence="ECO:0000269|PubMed:23221802"
SQ   SEQUENCE   301 AA;  33321 MW;  04638F36F26FADDC CRC64;
     MDILDKLVDL AQLTGSADVQ CLLGGQWSVR HETLQCEGLV HIVTAGSGYL CIDGETSPRP
     VGTGDIVFFP RGLGHVLSHD GKYGESLQPD IRQNGTFMVK QCGNGLDMSL FCARFRYDTH
     ADLMNGLPET VFLNIAHPSL QYVVSMLQLE SEKPLTGTVS VVNALPSVLL VLILRAYLEQ
     DKDVELSGVL KGWQDKRLGH LIQKVIDKPE DEWNIDKMVA AANMSRAQLM RRFKSQVGLS
     PHAFVNHIRL QKGALLLKKT PDSVLEVALS VGFQSETHFG KAFKRQYHVS PGQYRKEGGQ
     K