ID J2T1M4_9FLAO Unreviewed; 296 AA.
AC J2T1M4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=PMI13_02229 {ECO:0000313|EMBL:EJL71892.1};
OS Chryseobacterium populi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1144316 {ECO:0000313|EMBL:EJL71892.1, ECO:0000313|Proteomes:UP000007509};
RN [1] {ECO:0000313|EMBL:EJL71892.1, ECO:0000313|Proteomes:UP000007509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF314 {ECO:0000313|EMBL:EJL71892.1,
RC ECO:0000313|Proteomes:UP000007509};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL71892.1}.
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DR EMBL; AKJY01000035; EJL71892.1; -; Genomic_DNA.
DR AlphaFoldDB; J2T1M4; -.
DR PATRIC; fig|1144316.3.peg.2247; -.
DR Proteomes; UP000007509; 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 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 Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 296 AA; 32412 MW; A3BCB8697C052748 CRC64;
MMKPVGKLIV IGGAVNKGSF AETDFDQNIE KNLNFFERGI LRKIINESKH KENSVIEIIT
TASQIPQIVG TEYKKAFEFL GAKNVNILDI HNREEANSDA MVARASAADV VMFTGGDQLR
LTSILGGTRF HDTILLKYQE QDFIYSGTSA GAAAASENMI YQGSSSEALL KGEIKTTQGL
GLIDNVIIDT HFVQRGRIGR LFQAVVNNPR TLGIGLGEDT GLFIYNDVMT AVGSGLVIIV
DGRFIKDTNL TNINLGEPIS IDNLTVHVMS MNDHYDLTTK TLTIENSQFN PIPQDK
//
