ID K9QP63_NOSS7 Unreviewed; 334 AA.
AC K9QP63;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719, ECO:0000256|PIRNR:PIRNR032067};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115, ECO:0000256|PIRNR:PIRNR032067};
GN OrderedLocusNames=Nos7524_1332 {ECO:0000313|EMBL:AFY47213.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY47213.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi-
CC L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve
CC polymer) into aspartate-arginine dipeptides.
CC {ECO:0000256|ARBA:ARBA00002039, ECO:0000256|PIRNR:PIRNR032067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-
CC 2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspartate;
CC Xref=Rhea:RHEA:12845, Rhea:RHEA-COMP:13728, Rhea:RHEA-COMP:13734,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:137986, ChEBI:CHEBI:137991;
CC EC=3.4.15.6; Evidence={ECO:0000256|ARBA:ARBA00001092,
CC ECO:0000256|PIRNR:PIRNR032067};
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534, ECO:0000256|PIRNR:PIRNR032067}.
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DR EMBL; CP003552; AFY47213.1; -; Genomic_DNA.
DR RefSeq; WP_015137667.1; NC_019684.1.
DR AlphaFoldDB; K9QP63; -.
DR STRING; 28072.Nos7524_1332; -.
DR MEROPS; S51.003; -.
DR KEGG; nop:Nos7524_1332; -.
DR PATRIC; fig|28072.8.peg.1454; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_051822_0_0_3; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000010378; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03145; GAT1_cyanophycinase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR InterPro; IPR011811; Peptidase_S51_cyanophycinase.
DR PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR PIRSF; PIRSF032067; Cyanophycinase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR032067};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR032067};
KW Reference proteome {ECO:0000313|Proteomes:UP000010378};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR032067}.
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 334 AA; 37415 MW; 984D5BEEB306515F CRC64;
MTRAFPSIAR FLKATGTMLL RVISRLKAYL RFDFDSNTAE ILPTLAGPVF NLGGGGTDVE
AAIQWMINQV RGGANSPHKI NVVVIRTYGS DDYNRLIYSM KGVNSVATLI VSNRQDANRD
DILRKIRNAG VVFFAGGDQC QYIRSWKNTK LEAAVQSVYK RGGGIGGTSA GAMILSDFIY
DACACEDPIE TKDALEDPYQ NITFTYNFFR WHHLQGTIID THFDSRKRMG RIMAFIARQI
QDGVSRSALG IAISEETSIV VDKYGKAKVM GRNAAYFVLG DHPPEVCKPR TPLTYHDYKI
WRVPSGNTFD LNNPPSRGYY FRSVKRGRFD SDPY
//
