ID A0A0Q4LGW3_9SPHI Unreviewed; 280 AA.
AC A0A0Q4LGW3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=ASE92_03650 {ECO:0000313|EMBL:KQN38534.1};
OS Pedobacter sp. Leaf41.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736218 {ECO:0000313|EMBL:KQN38534.1, ECO:0000313|Proteomes:UP000051488};
RN [1] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQN38534.1}.
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DR EMBL; LMLE01000001; KQN38534.1; -; Genomic_DNA.
DR RefSeq; WP_056848711.1; NZ_LMLE01000001.1.
DR AlphaFoldDB; A0A0Q4LGW3; -.
DR STRING; 1736218.ASE92_03650; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000051488; Unassembled WGS sequence.
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 Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..280
FT /note="Cyanophycinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006225728"
SQ SEQUENCE 280 AA; 30862 MW; 5DC3CF703E68BD17 CRC64;
MKKLFLIFAL VGFSLMLNAQ SKATKGNLFI IGGGNRSDEL MKQMLNTAEL KPSDYIVVLP
MASEVPDVGF GTLSAQLQKL DPRVIKNFNF AEHDVNDKKW TDSLSSAKLI YILGGDQSRF
MNVVLNTPVY TAIHKAYQNG ATIAGTSAGA AVMSKYMITG KQLLDTVYKE TFNKLWDKNI
EFLPGMGLLE NTIIDQHFLK RNRYNRLISA LAAHPDLVCV GIDESTAIIV HGNKATVAGE
SQVVRLANPK ELKKTDKGLM KFKQSEFGIF TAGDVIDIKP
//
