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Database: UniProt
Entry: A0A0S1SF85_9FLAO
LinkDB: A0A0S1SF85_9FLAO
Original site: A0A0S1SF85_9FLAO 
ID   A0A0S1SF85_9FLAO        Unreviewed;       290 AA.
AC   A0A0S1SF85;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE            EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN   ORFNames=SB49_12660 {ECO:0000313|EMBL:ALM08560.1};
OS   Sediminicola sp. YIK13.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sediminicola.
OX   NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM08560.1, ECO:0000313|Proteomes:UP000063759};
RN   [1] {ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA   Kwon Y.M., Kim S.-J.;
RT   "Genome sequence of Sediminicola sp. YIK13.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALM08560.1, ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|EMBL:ALM08560.1,
RC   ECO:0000313|Proteomes:UP000063759};
RX   PubMed=26823585;
RA   Kwon Y.M., Kim S.J.;
RT   "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT   Bacterium Sediminicola sp. YIK13.";
RL   Genome Announc. 4:e01635-15(2016).
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}.
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   -!- SIMILARITY: Belongs to the peptidase S51 family.
CC       {ECO:0000256|ARBA:ARBA00006534}.
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DR   EMBL; CP010535; ALM08560.1; -; Genomic_DNA.
DR   RefSeq; WP_062057131.1; NZ_CP010535.1.
DR   AlphaFoldDB; A0A0S1SF85; -.
DR   STRING; 1453352.SB49_12660; -.
DR   KEGG; syi:SB49_12660; -.
DR   PATRIC; fig|1453352.4.peg.2648; -.
DR   OrthoDB; 9799980at2; -.
DR   Proteomes; UP000063759; 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   NCBIfam; TIGR02069; cyanophycinase; 1.
DR   PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR   PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063759};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..290
FT                   /note="Cyanophycinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006589559"
SQ   SEQUENCE   290 AA;  32516 MW;  A34ED15E5E48BF26 CRC64;
     MLKISFVLFI TLLLPIVSTA QENKVTTGNE NGTLIAIGGG DIGHTNIMKE FRKLAGGDSA
     KIVVIPTAFV RDNEIDTLLL KRNFREYGIP NFTVLHTNDS TEVNTDDFVK PIKEATGIYF
     TGGRHWRIAD SYLNTKVHKE LLKLLDRGGV IAGSSAGATI QGSYLARGDT KNNQIMMGDH
     EIGFGFISNI VIDQHVLSRN RQFDMFTILE KKPELLGVGI DESTAIVVKG DTLQVIGESY
     VIIYDKSFWS NEHNPFDEET QKKLPNKNQL FYFLKSGDKY NLRDRKVIRN
//
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