HETR_TRIV2
ID HETR_TRIV2 Reviewed; 299 AA.
AC Q9F5Y3; Q3MGV2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA-binding transcriptional activator HetR {ECO:0000255|HAMAP-Rule:MF_00781};
DE EC=3.4.21.- {ECO:0000255|HAMAP-Rule:MF_00781};
DE AltName: Full=Heterocyst differentiation control protein {ECO:0000255|HAMAP-Rule:MF_00781};
GN Name=hetR {ECO:0000255|HAMAP-Rule:MF_00781}; OrderedLocusNames=Ava_0158;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=12151106; DOI=10.1016/s0167-4781(02)00399-8;
RA Schiefer W., Schuetz K., Hachtel W., Happe T.;
RT "Molecular cloning and characterization of hetR genes from filamentous
RT cyanobacteria.";
RL Biochim. Biophys. Acta 1577:139-143(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
CC -!- FUNCTION: Controls heterocyst differentiation. Dimerization is required
CC for DNA-binding. Has both a protease and a DNA-binding activity.
CC {ECO:0000255|HAMAP-Rule:MF_00781, ECO:0000305|PubMed:12151106}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000255|HAMAP-
CC Rule:MF_00781}.
CC -!- DISRUPTION PHENOTYPE: Mutant strains no longer develop heterocysts when
CC grown in medium without combined nitrogen. Aerobically growing cells do
CC not express nitrogenase, and do not grow in the absence of exogenous
CC nitrogen. Cells grow normally under anaerobic conditions, even in the
CC absence of nitrogen. {ECO:0000269|PubMed:12151106}.
CC -!- SIMILARITY: Belongs to the peptidase S48 family. {ECO:0000255|HAMAP-
CC Rule:MF_00781}.
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DR EMBL; AF301157; AAG24634.2; -; Genomic_DNA.
DR EMBL; CP000117; ABA19784.1; -; Genomic_DNA.
DR RefSeq; WP_010996495.1; NC_007413.1.
DR AlphaFoldDB; Q9F5Y3; -.
DR SMR; Q9F5Y3; -.
DR STRING; 240292.Ava_0158; -.
DR MEROPS; S48.001; -.
DR EnsemblBacteria; ABA19784; ABA19784; Ava_0158.
DR GeneID; 58722805; -.
DR KEGG; ava:Ava_0158; -.
DR eggNOG; ENOG502Z96Q; Bacteria.
DR HOGENOM; CLU_926376_0_0_3; -.
DR OMA; HHIEPKR; -.
DR Proteomes; UP000002533; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043158; P:heterocyst differentiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1670; -; 1.
DR Gene3D; 1.10.10.1680; -; 1.
DR HAMAP; MF_00781; HetR; 1.
DR InterPro; IPR040949; HetR_C.
DR InterPro; IPR041936; HetR_DNA-bd_N.
DR InterPro; IPR041935; HetR_flap.
DR InterPro; IPR005319; Pept_S48_HetR.
DR Pfam; PF18460; HetR_C; 1.
DR Pfam; PF03574; Peptidase_S48; 1.
PE 3: Inferred from homology;
KW Activator; Disulfide bond; DNA-binding; Heterocyst; Hydrolase; Protease;
KW Serine protease; Transcription; Transcription regulation.
FT CHAIN 1..299
FT /note="DNA-binding transcriptional activator HetR"
FT /id="PRO_0000208479"
FT ACT_SITE 152
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00781"
FT DISULFID 48
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00781"
FT CONFLICT 2
FT /note="S -> V (in Ref. 1; AAG24634)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="S -> G (in Ref. 1; AAG24634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34969 MW; 74AF6CA9D87F9126 CRC64;
MSNDIDLIKR LGPSAMDQIM LYLAFSAMRT SGHRHGAFLD AAATAAKCAI YMTYLEQGQN
LRMTGHLHHL EPKRVKIIVE EVRQALMEGK LLKTLGSQEP RYLIQFPYVW MEQYPWIPGR
SRIPGTSLTS EEKRQIEHKL PSNLPDAQLV TSFEFLELIE FLHKRSQEDL PPEHRMELSE
ALAEHIKRRL LYSGTVTRID SPWGMPFYAL TRPFYAPADD QERTYIMVED TARYFRMMKD
WAEKRPNAMR ALEELDVPPE RWDEAMQELD EIIRTWADKY HQVGGIPMIL QMVFGRKED