ID A0A259TVN8_9BACT Unreviewed; 968 AA.
AC A0A259TVN8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cyanophycin synthetase {ECO:0000256|ARBA:ARBA00022036};
DE EC=6.3.2.29 {ECO:0000256|ARBA:ARBA00013005};
DE EC=6.3.2.30 {ECO:0000256|ARBA:ARBA00012968};
DE AltName: Full=Cyanophycin synthase {ECO:0000256|ARBA:ARBA00031353};
GN ORFNames=BSZ36_01790 {ECO:0000313|EMBL:OZC01829.1};
OS Rubricoccus marinus.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubricoccus.
OX NCBI_TaxID=716817 {ECO:0000313|EMBL:OZC01829.1, ECO:0000313|Proteomes:UP000216446};
RN [1] {ECO:0000313|EMBL:OZC01829.1, ECO:0000313|Proteomes:UP000216446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-29 {ECO:0000313|EMBL:OZC01829.1,
RC ECO:0000313|Proteomes:UP000216446};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003184}.
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 Evidence={ECO:0000256|ARBA:ARBA00000535};
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 Evidence={ECO:0000256|ARBA:ARBA00000917};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000256|ARBA:ARBA00009060}.
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:OZC01829.1}.
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DR EMBL; MQWB01000001; OZC01829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259TVN8; -.
DR InParanoid; A0A259TVN8; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000216446; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 NCBIfam; TIGR02068; cya_phycin_syn; 1.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000216446}.
FT DOMAIN 232..487
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 922..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 105647 MW; F940D0E72D52E265 CRC64;
MRILSTNVYV GPNVYARFPV IRHVIDLGPL ENYPTGTLGD FPARLVEALP GLQEHGCSYR
EPGGFIRRMT EDEGTWLGHV WEHVALELQG IAGSDVTFGK TRSRRGEPGC YDMVYSYHQR
EVGLEAGKLA RRLILQLLPP EVQAEIDEEK EDWDWDEERD DFIRFAQRRE FGPSTQSIVD
AAVARGIPWL RLNKYSLVQF GHGKYQKRIQ ATVTSETKHI SVELASDKDE THSLLGDLGL
PVPKQTLCYS VRDAIRAAEK TGYPVVVKPL NANHGRGVSI RLMTPEAVET GFHVASEHGT
SRGVLVESFV EGFDHRMLVV GGKLIAVAKR VPGHVVGDGT HTIEELVEIV NADPRRGVGH
EKVLTQLQFD EQAERLMEKR GVTKETVLAS GETLFLRETA NLSTGGTAID LTDVVHPDNR
DMAERAIKAI GLDVGGVDFL STDITKSWRD IGGGIVECNA APGFRMHVAP SEGTPRNVAE
PVIDLLFPPG TPARIPIAAI TGTNGKTTTT RMLAHIAQMA GYTPGMTTSD GVYINGRMSV
KGDMTGPTSS NMVLRDPDVD CAILETARGG MVRSGLAFNE CDVAACLNVR ADHLGIRGID
TLDQLAEIKK IPIDVAKDCA VLNADDERCL AMAADSRAES ICYVTMDPQH AIVREHVRAG
GRAVVLEPGM NGDMITIYDG GRHIPLLWTH LIPATMEGKA THNVQNAMFA AGMAYALGEN
AMEKINLDHI RHGLRTFSTS YYEAPGRLNV FDEHPFKVIL DYAHNPDAVG MMVELAGKLD
VRGKRRLVLA APGDRRDEDI REIATIAAGH FDHYVCKRDD NPRGRDEREV PLMLQKALLD
AGVAPEAVDI VVDEQEAIEH ALASGEENDL ILIFGDDISR SWKQIIYFGQ ASGDGEDETA
PPTPVTAPML APEASGGMIA APATASAKPA KGPITRRDAD MDAVDLPDGQ RLVRDERGVR
IVLDEEAD
//
