ID A0A1S6FKU5_9SPHN Unreviewed; 338 AA.
AC A0A1S6FKU5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=BXU08_11625 {ECO:0000313|EMBL:AQR74215.1};
OS Sphingomonas sp. LM7.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1938607 {ECO:0000313|EMBL:AQR74215.1, ECO:0000313|Proteomes:UP000189383};
RN [1] {ECO:0000313|EMBL:AQR74215.1, ECO:0000313|Proteomes:UP000189383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM7 {ECO:0000313|EMBL:AQR74215.1,
RC ECO:0000313|Proteomes:UP000189383};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019511; AQR74215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6FKU5; -.
DR STRING; 1938607.BXU08_11625; -.
DR KEGG; splm:BXU08_11625; -.
DR Proteomes; UP000189383; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000189383};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..338
FT /note="Cyanophycinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013068725"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 338 AA; 35179 MW; 17ACE09A9B2F00FD CRC64;
MKPLLRPLAV FLALLLALPG HAQAPVGYAY YEVGDVAAKT PKPTAQALML MGGGEWDLGA
FRWFAERAGN GHIVVLRASG AGDAGEEIFR DVGGVLSVQT IVFSDRAAAS DPRVLDVLAR
ADGIFLAGGD QANYVRYWKD TPVARLLDAH VAKGRPIAGT SAGLAILGGT AYGAMDGGSI
DSPSALADPA GPGVTLVTGF LSMPRLAHVV TDTHFNARDR LGRLIAFLAA ARQTDAAVIG
IGVDEQSALC VEADGTARLR TRNGGFAWLV RPRNKPVIAL GTPLDWSDVE VTGIGPDSRF
DLESLRVGDP VFSGVARVVG GRLLDAPKAP GVVTASLR
//
