ID   AMRZ_PSEAE              Reviewed;         108 AA.
AC   G3XCY4;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Transcription factor AmrZ {ECO:0000303|PubMed:22511872};
DE   AltName: Full=Alginate and motility regulator Z;
GN   Name=amrZ {ECO:0000303|PubMed:16352829}; OrderedLocusNames=PA3385;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=FRD1;
RX   PubMed=10476040; DOI=10.1046/j.1365-2958.1999.01550.x;
RA   Baynham P.J., Brown A.L., Hall L.L., Wozniak D.J.;
RT   "Pseudomonas aeruginosa AlgZ, a ribbon-helix-helix DNA-binding protein, is
RT   essential for alginate synthesis and algD transcriptional activation.";
RL   Mol. Microbiol. 33:1069-1080(1999).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF ARG-22.
RC   STRAIN=FRD1;
RX   PubMed=15968052; DOI=10.1128/jb.187.13.4430-4443.2005;
RA   Ramsey D.M., Baynham P.J., Wozniak D.J.;
RT   "Binding of Pseudomonas aeruginosa AlgZ to sites upstream of the algZ
RT   promoter leads to repression of transcription.";
RL   J. Bacteriol. 187:4430-4443(2005).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-18 AND ARG-22.
RX   PubMed=16352829; DOI=10.1128/jb.188.1.132-140.2006;
RA   Baynham P.J., Ramsey D.M., Gvozdyev B.V., Cordonnier E.M., Wozniak D.J.;
RT   "The Pseudomonas aeruginosa ribbon-helix-helix DNA-binding protein AlgZ
RT   (AmrZ) controls twitching motility and biogenesis of type IV pili.";
RL   J. Bacteriol. 188:132-140(2006).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF ARG-22.
RX   PubMed=23354748; DOI=10.1128/jb.02190-12;
RA   Jones C.J., Ryder C.R., Mann E.E., Wozniak D.J.;
RT   "AmrZ modulates Pseudomonas aeruginosa biofilm architecture by directly
RT   repressing transcription of the psl operon.";
RL   J. Bacteriol. 195:1637-1644(2013).
RN   [6]
RP   FUNCTION, SUBUNIT, AND DOMAIN.
RX   PubMed=26549743; DOI=10.1111/1758-2229.12354;
RA   Xu B., Ju Y., Soukup R.J., Ramsey D.M., Fishel R., Wysocki V.H.,
RA   Wozniak D.J.;
RT   "The Pseudomonas aeruginosa AmrZ C-terminal domain mediates tetramerization
RT   and is required for its activator and repressor functions.";
RL   Environ. Microbiol. Rep. 8:85-90(2016).
RN   [7]
RP   FUNCTION.
RX   PubMed=28673999; DOI=10.1073/pnas.1700286114;
RA   Allsopp L.P., Wood T.E., Howard S.A., Maggiorelli F., Nolan L.M.,
RA   Wettstadt S., Filloux A.;
RT   "RsmA and AmrZ orchestrate the assembly of all three type VI secretion
RT   systems in Pseudomonas aeruginosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:7707-7712(2017).
RN   [8] {ECO:0007744|PDB:3QOQ}
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-66 IN COMPLEX WITH DNA, AND
RP   FUNCTION.
RX   PubMed=22511872; DOI=10.1371/journal.ppat.1002648;
RA   Pryor E.E., Waligora E.A., Xu B., Dellos-Nolan S., Wozniak D.J., Hollis T.;
RT   "The transcription factor AmrZ utilizes multiple DNA binding modes to
RT   recognize activator and repressor sequences of Pseudomonas aeruginosa
RT   virulence genes.";
RL   PLoS Pathog. 8:E1002648-E1002648(2012).
CC   -!- FUNCTION: Functions as both a transcriptional activator and repressor
CC       of multiple genes encoding virulence factors as well as genes involved
CC       in environmental adaptation (PubMed:16352829, PubMed:26549743,
CC       PubMed:22511872). Plays a role in alginate production via the
CC       activation of AlgD which is the first gene in the alginate biosynthetic
CC       operon (PubMed:16352829, PubMed:10476040). Regulates also the
CC       transcription of genes responsible for type IV pili localization and
CC       twitching motility (PubMed:16352829). Mediates transition of
CC       P.aeruginosa biofilm infections from colonizing to chronic biofilms
CC       through repression of the psl operon (PubMed:23354748). Represses also
CC       its own transcription by binding to two sites on amrZ promoter, amrZ1
CC       and amrZ2 (PubMed:15968052). {ECO:0000269|PubMed:10476040,
CC       ECO:0000269|PubMed:15968052, ECO:0000269|PubMed:16352829,
CC       ECO:0000269|PubMed:22511872, ECO:0000269|PubMed:23354748,
CC       ECO:0000269|PubMed:26549743}.
CC   -!- SUBUNIT: Forms homotetramers (via C-terminus).
CC       {ECO:0000269|PubMed:26549743}.
CC   -!- DOMAIN: The C-terminal is essential for tetramerization as well as
CC       efficient AmrZ-mediated activation and repression of its targets.
CC       {ECO:0000269|PubMed:26549743}.
CC   -!- DISRUPTION PHENOTYPE: Deletion strain produces no detectable surface
CC       pili (PubMed:16352829). Abolishes also mucoidy and algD transcription
CC       (PubMed:10476040). {ECO:0000269|PubMed:10476040,
CC       ECO:0000269|PubMed:16352829}.
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DR   EMBL; AE004091; AAG06773.1; -; Genomic_DNA.
DR   PIR; D83221; D83221.
DR   RefSeq; NP_252075.1; NC_002516.2.
DR   RefSeq; WP_003091802.1; NZ_QZGE01000017.1.
DR   PDB; 3QOQ; X-ray; 3.10 A; A/B/C/D=1-66.
DR   PDBsum; 3QOQ; -.
DR   AlphaFoldDB; G3XCY4; -.
DR   SMR; G3XCY4; -.
DR   STRING; 287.DR97_4537; -.
DR   PaxDb; G3XCY4; -.
DR   PRIDE; G3XCY4; -.
DR   DNASU; 878714; -.
DR   EnsemblBacteria; AAG06773; AAG06773; PA3385.
DR   GeneID; 878714; -.
DR   KEGG; pae:PA3385; -.
DR   PATRIC; fig|208964.12.peg.3544; -.
DR   PseudoCAP; PA3385; -.
DR   HOGENOM; CLU_148670_1_0_6; -.
DR   OMA; NDSHRSM; -.
DR   PhylomeDB; G3XCY4; -.
DR   BioCyc; PAER208964:G1FZ6-3451-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   CollecTF; EXPREG_000004d0; -.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
DR   GO; GO:0003677; F:DNA binding; IDA:PseudoCAP.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR   GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:PseudoCAP.
DR   GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IMP:PseudoCAP.
DR   GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR   GO; GO:2000147; P:positive regulation of cell motility; IMP:PseudoCAP.
DR   GO; GO:1900233; P:positive regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR   GO; GO:0032885; P:regulation of polysaccharide biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
DR   Gene3D; 1.10.1220.10; -; 1.
DR   InterPro; IPR005569; Arc_DNA-bd_dom.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   Pfam; PF03869; Arc; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..108
FT                   /note="Transcription factor AmrZ"
FT                   /id="PRO_0000448532"
FT   MUTAGEN         18
FT                   /note="K->A: Complete loss of DNA-binding activity."
FT                   /evidence="ECO:0000269|PubMed:16352829"
FT   MUTAGEN         22
FT                   /note="R->A: Complete loss of DNA-binding activity."
FT                   /evidence="ECO:0000269|PubMed:15968052,
FT                   ECO:0000269|PubMed:16352829, ECO:0000269|PubMed:23354748"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:3QOQ"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:3QOQ"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:3QOQ"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:3QOQ"
SQ   SEQUENCE   108 AA;  12333 MW;  477A5C6873A73441 CRC64;
     MRPLKQATPT YSSRTADKFV VRLPEGMREQ IAEVARSHHR SMNSEIIARL EQSLLQEGAL
     QDNLGVRLDS PELSLHEREL LQRFRQLTHR QQNALVALIA HDAELAQA