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
//