CPHA_CROS5
ID CPHA_CROS5 Reviewed; 872 AA.
AC Q9KGY4; B1WPL7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cyanophycin synthetase;
DE EC=6.3.2.29;
DE EC=6.3.2.30;
DE AltName: Full=Cyanophycin synthase;
GN Name=cphA; OrderedLocusNames=cce_2237;
OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS ATCC 51142)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX NCBI_TaxID=43989;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li H., Sherman D.M., Bao S., Sherman L.A.;
RT "Cyanophycin dynamics in diazatrophic and non-diazatrophic cyanobacteria.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51142 / BH68;
RX PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT important in the marine nitrogen cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC -!- FUNCTION: Catalyzes the ATP-dependent polymerization of arginine and
CC aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a
CC water-insoluble reserve polymer). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-
CC 4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:13277, Rhea:RHEA-COMP:13728, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.29;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ATP + L-
CC arginine = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23888, Rhea:RHEA-COMP:13732, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.30;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000305}.
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DR EMBL; AF279247; AAF97933.1; -; Genomic_DNA.
DR EMBL; CP000806; ACB51587.1; -; Genomic_DNA.
DR RefSeq; WP_009546983.1; NC_010546.1.
DR AlphaFoldDB; Q9KGY4; -.
DR SMR; Q9KGY4; -.
DR STRING; 43989.cce_2237; -.
DR PRIDE; Q9KGY4; -.
DR EnsemblBacteria; ACB51587; ACB51587; cce_2237.
DR KEGG; cyt:cce_2237; -.
DR eggNOG; COG0769; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_016806_0_0_3; -.
DR OMA; PFMIANA; -.
DR OrthoDB; 1861122at2; -.
DR BRENDA; 6.3.2.29; 8115.
DR BRENDA; 6.3.2.30; 8115.
DR Proteomes; UP000001203; Chromosome circular.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0071161; F:cyanophycin synthetase activity (L-arginine-adding); IEA:UniProtKB-EC.
DR GO; GO:0071160; F:cyanophycin synthetase activity (L-aspartate-adding); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011810; Cya_phycin_syn.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR02068; cya_phycin_syn; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..872
FT /note="Cyanophycin synthetase"
FT /id="PRO_0000101713"
FT DOMAIN 224..480
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 495..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 872 AA; 95230 MW; 6325018DC2724BA7 CRC64;
MKILKTLTLR GPNYWSIRRK KLIVMRLDLE DLADKPSNEI PGFYDGLVEV LPSLVEHYCS
PGHRGGFLER VKEGTYMGHI VEHVALELQE LTKMPVGFGR TRETATPGIY NVVFEYVDEQ
AGRYAGRAAV RLCRSIVDTG TYPLKELEQD LSDLQDLQAN ASLGPSTQTL VTEAEARNIP
WMALSARAMV QLGYGVHQKR IQATLSNYSG ILAVELACDK EGTKTILQDA GVPVPRGTTI
QFFEELESAI DDVGGYPIVI KPLDGNHGRG ITIDINSWKE AEEAYDLASE ESKTRTVIVE
RFYKGSDHRL LVINGKLVAV AERVPAHVIG DDKHTIEELI DITNEDPRRG EGHDNVLTRI
KVDKTVLGML DKQGLRLDSI LDKGEIVYLR ATANLSTGGS AIDRTDDIHP ENLWMAERVA
KIIGLDIMGI DVVTPDITKP LRDVDGVIVE VNAAPGFRMH VAPSQGLSRN VAAPVMDMLF
PPESPSRVPI VAITGTNGKT TTTRLTAHIY RQTGKVVGYT STDGVYIGEY LVEKGDNTGP
FSAGMILKDP TVEVAVLESA RGGILRSGLA FDTCDVGIVL NVAADHLGLG DINTIEQMAR
VKGVVAEVVH ADGYAVLNAD DPLVAAMAEQ VKGKVAYFSM NPDNEIIHNH TRRDGMAAVY
ENGYISILEG QFTLRIEEAV NVPMTMGGMA PFMIANALAA CLAAFCQGVD IEDIRQGVRT
FKASANQTPG RMNLFNLGDY HALVDYAHNP AGYEAVGEFV KNWKGQRLGV VGGPGDRRDE
DLILLGKIAA RVFDRILVKE DDDKRGRARG EAADLIIDGI LSENDKADYE AILDETEAIE
YGLDKVDKGG LVVIFPESVT RAISLINRRN PI
