PATS_NOSS1
ID PATS_NOSS1 Reviewed; 17 AA.
AC O52748;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Transcriptional regulator peptide PatS;
DE AltName: Full=Heterocyst inhibition-signaling peptide;
DE Contains:
DE RecName: Full=PatS6;
GN Name=patS {ECO:0000303|PubMed:9794762}; OrderedLocusNames=asl2301;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, INDUCTION BY NITROGEN LIMITATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ARG-13; SER-15; GLY-16 AND ARG-17.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=9794762; DOI=10.1126/science.282.5390.935;
RA Yoon H.-S., Golden J.W.;
RT "Heterocyst pattern formation controlled by a diffusible peptide.";
RL Science 282:935-938(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY NITROGEN LIMITATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11274121; DOI=10.1128/jb.183.8.2605-2613.2001;
RA Yoon H.S., Golden J.W.;
RT "PatS and products of nitrogen fixation control heterocyst pattern.";
RL J. Bacteriol. 183:2605-2613(2001).
RN [4]
RP FUNCTION IN INHIBITION OF DNA-BINDING OF HETR, AND INDUCTION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=15051891; DOI=10.1073/pnas.0400429101;
RA Huang X., Dong Y., Zhao J.;
RT "HetR homodimer is a DNA-binding protein required for heterocyst
RT differentiation, and the DNA-binding activity is inhibited by PatS.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4848-4853(2004).
RN [5] {ECO:0007744|PDB:4YNL}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 12-17 IN COMPLEX WITH HETR,
RP FUNCTION, PROBABLE MATURE PEPTIDE, AND SUBUNIT.
RX PubMed=26576507; DOI=10.1038/srep16470;
RA Hu H.X., Jiang Y.L., Zhao M.X., Cai K., Liu S., Wen B., Lv P., Zhang Y.,
RA Peng J., Zhong H., Yu H.M., Ren Y.M., Zhang Z., Tian C., Wu Q.,
RA Oliveberg M., Zhang C.C., Chen Y., Zhou C.Z.;
RT "Structural insights into HetR-PatS interaction involved in cyanobacterial
RT pattern formation.";
RL Sci. Rep. 5:16470-16470(2015).
CC -!- FUNCTION: Inhibits heterocyst differentiation; a peptide corresponding
CC to the last 5-6 amino acids blocks heterocyst formation when added
CC exogenously in culture. Controls heterocyst pattern formation through
CC intercellular signaling mechanisms. In Nostoc filaments, approximately
CC every 10th vegetative cell terminally differentiates into a heterocyst
CC specialized for nitrogen fixation. Seems to inhibit the formation of
CC adjacent heterocysts (PubMed:9794762, PubMed:11274121,
CC PubMed:15051891). The C-terminal peptide binds HetR, inhibits hetR
CC transcription and blocks the DNA-binding of HetR. Peptide binding to
CC HetR alters its conformation, probably leading to dissociation of the
CC HetR-DNA complex and cessation of transcription (PubMed:26576507).
CC {ECO:0000269|PubMed:11274121, ECO:0000269|PubMed:15051891,
CC ECO:0000269|PubMed:26576507, ECO:0000269|PubMed:9794762}.
CC -!- SUBUNIT: The C-terminal peptide binds HetR; one peptide binds to each
CC subunit of the HetR homodimer. {ECO:0000269|PubMed:26576507}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:9794762}.
CC Note=Probably diffuses to adjacent cells. {ECO:0000305|PubMed:9794762}.
CC -!- DEVELOPMENTAL STAGE: Expressed in proheterocysts (at protein level).
CC {ECO:0000269|PubMed:11274121, ECO:0000269|PubMed:9794762}.
CC -!- INDUCTION: Transcribed at low levels in vegetative cells
CC (PubMed:11274121). Under control of HetR (PubMed:15051891).
CC Transcription and translation rises 3-fold by 6 hours after heterocyst
CC induction by nitrogen reduction (before proheterocysts can be
CC identified), descends to preinduction levels by 27 hours (at protein
CC level) (PubMed:9794762, PubMed:11274121). {ECO:0000269|PubMed:11274121,
CC ECO:0000269|PubMed:15051891, ECO:0000269|PubMed:9794762}.
CC -!- DISRUPTION PHENOTYPE: Forms multiple, contiguous heterocysts with
CC abnormal short spacing between heterocysts on nitrogen-containing
CC medium. These heterocysts do not have nitrogenase activity
CC (PubMed:9794762, PubMed:11274121). In nitrogen-free medium nearly
CC normal heterocyst patterns are established after 4 days growth
CC (PubMed:11274121). {ECO:0000269|PubMed:11274121,
CC ECO:0000269|PubMed:9794762}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Heterocyst or not
CC heterocyst? - Issue 23 of June 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/023";
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DR EMBL; AF046871; AAC03103.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB74000.1; -; Genomic_DNA.
DR PIR; AF2093; AF2093.
DR PDB; 4YNL; X-ray; 2.10 A; C/D/P/R=12-17.
DR PDBsum; 4YNL; -.
DR AlphaFoldDB; O52748; -.
DR SMR; O52748; -.
DR EnsemblBacteria; BAB74000; BAB74000; BAB74000.
DR KEGG; ana:asl2301; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0043158; P:heterocyst differentiation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Heterocyst; Periplasm; Reference proteome; Transcription;
KW Transcription regulation.
FT PEPTIDE 1..17
FT /note="Transcriptional regulator peptide PatS"
FT /id="PRO_0000044184"
FT PEPTIDE 12..17
FT /note="PatS6"
FT /evidence="ECO:0000305|PubMed:26576507"
FT /id="PRO_0000452151"
FT MUTAGEN 13
FT /note="R->C: Does not inhibit heterocyst formation."
FT /evidence="ECO:0000269|PubMed:9794762"
FT MUTAGEN 15
FT /note="S->D: Does not inhibit heterocyst formation."
FT /evidence="ECO:0000269|PubMed:9794762"
FT MUTAGEN 16
FT /note="G->S: Does not inhibit heterocyst formation."
FT /evidence="ECO:0000269|PubMed:9794762"
FT MUTAGEN 17
FT /note="R->L: Does not inhibit heterocyst formation."
FT /evidence="ECO:0000269|PubMed:9794762"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4YNL"
SQ SEQUENCE 17 AA; 1927 MW; 192BE168476867F3 CRC64;
MKAIMLVNFC DERGSGR
