ID A0A1B3XLD9_9BACI Unreviewed; 873 AA.
AC A0A1B3XLD9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 18-JUN-2025, entry version 33.
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=ABE28_006715 {ECO:0000313|EMBL:AOH54038.1};
OS Peribacillus muralis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Peribacillus.
OX NCBI_TaxID=264697 {ECO:0000313|EMBL:AOH54038.1, ECO:0000313|Proteomes:UP000077926};
RN [1] {ECO:0000313|EMBL:AOH54038.1, ECO:0000313|Proteomes:UP000077926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-68 {ECO:0000313|EMBL:AOH54038.1,
RC ECO:0000313|Proteomes:UP000077926};
RA Zheng Z.;
RT "Complete genome sequence of Bacillus muralis G25-68, a strain with
RT toxicity to nematodes.";
RL Submitted (AUG-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) + L-aspartate + ATP = [L-
CC 4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + phosphate +
CC H(+); 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:ARBA00048425};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + L-arginine
CC + ATP = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + phosphate +
CC H(+); 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:ARBA00048094};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000256|ARBA:ARBA00009060}.
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DR EMBL; CP017080; AOH54038.1; -; Genomic_DNA.
DR RefSeq; WP_064466489.1; NZ_CP017080.1.
DR AlphaFoldDB; A0A1B3XLD9; -.
DR STRING; 264697.ABE28_006715; -.
DR KEGG; bmur:ABE28_006715; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000077926; 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:0009058; P: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; IPR013651; ATP-grasp_RimK-type.
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 NCBIfam; NF010623; PRK14016.1; 1.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF08443; RimK; 2.
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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000077926}.
FT DOMAIN 220..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 873 AA; 96493 MW; 212AE2B5FACF38F2 CRC64;
MIINRVRYLK GPNYFAYTPT ICIELDLEEL EEKPSDTISG FNEKLLNALP NLGNHTCSKG
YRGGFAERLR QGTWMAHILE HMAIELQNMA GIDVIRGKTV MMEKKGHYQV TFEYQEPEAG
LQAFLAAKEI AEAILKGEKE VHVQSYVKKI EDLYYKNKLG PSTEAIFMAA QKKNIPVERI
GEDSLLRLGT GSRQKYVQAT ISSQTSSIAV ENACDKSLTK SILKGCGLPV PEGAIAHSIE
EIFDAADRLG FPLVIKPYNG RQGQGVITHI KNKDELFNVI NCLEAYVEKF IVERHIEGHD
YRLLIVNGEL LATSLRLPPY VIGNGKETIR RLIEKENRNS LRGNGHEKPM SKIPLTHTVT
CYLEKTNRTL GSIPKQGELV QVAGNANLST GGKAIDVTEQ VHPTIKKMAV AAAKAIGLDI
AGIDFICEDI SMPLDHSRTA IIEVNAAPGI RMHHYPSEGK KRDVGKAIID YLFPSREDAA
IPIIAVTGTN GKTTTTRMIH YFLSNDKTMV GMTNSDGVYI GEEIVDQGDC SGPISAGMVL
AHPEVDVAVL ETARGGILRE GLAFRQCNVG IITNVSEDHL GCDGMDTMED LVKLKRLIAE
VVMDTGYCIL NADDPKVAQM GAYTDGEVIY TSTDPSQPLV KEAIKGGQKV WFVNEQGMIL
HSSDSVTQPF MECTEIPITI SGMARHNIAN LLQALAAAHT QGISLDELRK KAVTFMPDTN
LSKGRFNLKK LNERTIIIDY AHNEAGLKAI FETVSAYNRK HLITVLAGPG DRVDEELIRL
AKAAAIHSDL FIIKEDDDLR GRKPFEVAEL LQEAAVEAGL HKDRTRIVLN ELDAFVNAWE
ASRPGDLLLF FYTDFEYVEK FFQKVSSNRL SAQ
//
