ID A0A1J0KW00_9GAMM Unreviewed; 941 AA.
AC A0A1J0KW00;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Name=cphA {ECO:0000313|EMBL:APC97895.1};
GN ORFNames=KX01_1033 {ECO:0000313|EMBL:APC97895.1};
OS Francisella frigiditurris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=1542390 {ECO:0000313|EMBL:APC97895.1, ECO:0000313|Proteomes:UP000182521};
RN [1] {ECO:0000313|Proteomes:UP000182521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA97-1460 {ECO:0000313|Proteomes:UP000182521};
RA Kuske C.R., Challacombe J.F., Daligault H.E., Davenport K.W., Johnson S.L.,
RA Siddaramappa S., Petersen J.M.;
RL Submitted (OCT-2014) 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 ---------------------------------------------------------------------------
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; CP009654; APC97895.1; -; Genomic_DNA.
DR RefSeq; WP_071663960.1; NZ_CP009654.1.
DR AlphaFoldDB; A0A1J0KW00; -.
DR STRING; 1542390.KX01_1033; -.
DR KEGG; frc:KX01_1033; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000182521; Chromosome.
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; 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; PF13549; ATP-grasp_5; 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 Ligase {ECO:0000313|EMBL:APC97895.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 232..485
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 941 AA; 103565 MW; EB443335C4D2EE4D CRC64;
MKVLATNVYV GPNIYANFPV IRSEIDLGVL EEWPSAKIGT EFVDKLVENL PGLKEHGCSY
REEGGFIRRL KEDEGTWMGH IWEHVILELQ SMAGSDVTFG RTRSTGEPGH YNMVYEYKQK
DVGLRAMELA RELLLSILPQ QLQEEVGYKA DDFDFEYEKV KFIKFAQSKE FGPSTGSLVE
AAKKRDIPYI RLNDQSLVQF GHGKYQQRIQ ATITSQTTNI AVQMSCDKEQ TNKILGALGL
PVPQQKMVRT EADALRAAQK LGFPLVVKPL DGNHGRGISI NLKTYEEIRE AFVEASKVSR
YVLVEQYATG FDHRMLVVNG KLVAVAKRVP GHVVGDGKST IEELVEIVNQ DPRRGIGHEK
VLTILELDYQ ANTLMKAAGY NKDTILKEGE IFYLRSTANL STGGTAIDVT DIVHPDNRDM
AERAIRAIGL DVGGVDFLID DIAQSYHEIG GAICECNAAP GFRMHVAPSE GQPRDVAGAV
IDMLFPKELG NARIPIAAIT GTNGKTTTSR MVAHMWKNAG KVVGLTTTDG IYINGKLTVS
GDTTGPASAQ MVLRDPTVEM AILETARGGL VRSGMGYDYC NVGACLNIAS DHLGLKGVNT
LEDLAKVKSV VVEAAKDVAV LNADDPHCLK MSAKVTAKNI FYVTMNPEHA LVRQHIRAGG
KAVVIEKGVN GDMITIFDNH IHIPVLWTHL IPATMEGKAI HNVQNSMFAI AISYSMGMSL
DNIRDGLRTF VTSFYQAPGR MNWFEEHNFK VLMDYGHNPA AIKLVGHMIS NMDFTGKKIC
VIASPGDRRN EDIHELAAAA APHFDYFICK RDDDLRGRKP EEVPEMLKAG LIKAGISAEN
IEIIQDEVEA VNTALSMAEE GDLVTIFADK LKRTWKQIIY FNREDDEVEK GEVKTKTHEP
FSASVIAQDP SLSKEISEVI KAGIISDGSG VRVASFDEDS D
//