ID K9XPF1_STAC7 Unreviewed; 288 AA.
AC K9XPF1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=Sta7437_0314 {ECO:0000313|EMBL:AFZ33926.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ33926.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
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; CP003653; AFZ33926.1; -; Genomic_DNA.
DR AlphaFoldDB; K9XPF1; -.
DR STRING; 111780.Sta7437_0314; -.
DR KEGG; scs:Sta7437_0314; -.
DR PATRIC; fig|111780.3.peg.324; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_053928_0_0_3; -.
DR OMA; FMTGGDQ; -.
DR Proteomes; UP000010473; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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 NCBIfam; TIGR02069; cyanophycinase; 1.
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 Carboxypeptidase {ECO:0000313|EMBL:AFZ33926.1};
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:UP000010473};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR032067}.
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 288 AA; 31496 MW; 18B933D39FEB8414 CRC64;
MLQMPTMQNR ETQLQSSYTP ALTKTAILVI GGAEDKVHGR EILHTFFNRS GGSEAVIGII
PSASREPTII GDRYVQIFEE MGTKYTKVLD VRDRDQGNDS VYLDYVEECT GIFLTGGDQL
RLCGLLAETP LMDRIITRAQ NHEITVGGTS AGAAVMGYHM IAGGSSGESP NRSLVDMAMG
LGIIPEILVD QHFHNRNRLA RLLSAIASHS ELLGIGIDED TCAMFESDRT IQVLGKGTVT
IIDARSMSYT NQSQVKGSEP LSIHNLKLHV LCHGERYDLN SHQALPLK
//