ID A0A1S2RA53_9BACI Unreviewed; 873 AA.
AC A0A1S2RA53;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 27.
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=BIV59_03055 {ECO:0000313|EMBL:OIK14527.1};
OS Bacillus sp. MUM 13.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK14527.1, ECO:0000313|Proteomes:UP000180199};
RN [1] {ECO:0000313|EMBL:OIK14527.1, ECO:0000313|Proteomes:UP000180199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 13 {ECO:0000313|EMBL:OIK14527.1,
RC ECO:0000313|Proteomes:UP000180199};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 13.";
RL Submitted (OCT-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}.
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:OIK14527.1}.
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DR EMBL; MLYQ01000007; OIK14527.1; -; Genomic_DNA.
DR RefSeq; WP_071349974.1; NZ_MLYQ01000007.1.
DR AlphaFoldDB; A0A1S2RA53; -.
DR Proteomes; UP000180199; 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:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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; 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:UP000180199}.
FT DOMAIN 220..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 873 AA; 96470 MW; B6C72742939E2924 CRC64;
MKINCVKYLK GPNYFTYSPS IFIECDIEEL EYRPSDSIPG FTETLLKLLP GLKKHTCSPG
YEGGFAERLA SGTWMGHILE HIAIEIQVSA GIDVKRGKTL TGNQPGIYYI TYSYKEEKSG
LFAFEAAVEI IKSILADEKN IPVNDFIEKT AALFYKNKLG PSTEAIYEAA LAAKIPVQRV
GTESMLRLGT GSRQKFLQAT ISSQTSNIAV ETSCNKQLTK ETLQACGIPV PQGEVVASMS
EIFHTADRLG FPLVIKPLNG RQGQGVITNI KNKDELFNVV NCLGKHEDTY ILERYFEGND
YRLLVVDDKL AAASMRTAPF IIGNGKDSIR NLIEEENLNP LRGDGHEKPM SKIPLNHSVS
CFLEKFDLTL ESIPEKGKII AVAGNANLST GGRASDVTEQ VHPSIAKMAI SAAKAIGLDI
AGIDLICKDI SKPVNINEMA IIEINAAPGI RMHLYPSEGE MRDVGKTIVD YLFPDRREAA
IPIISITGTN GKTTTARLVH HFLSKEGIAV GMANSDGVFI GQQCLHQGDC SGPISARQVL
NHPMADFAVL ETARGGILRE GLAFRNCEVG IVTNVAEDHL GSDAIDTFEQ LVKLKRLIPE
VVHEEGYCIL NADDEQVAKM APYSKGEVIY TSINEHCRYI QNAIKNGKKA WFLNHDSWVV
YHDGNELIMF LDCRDIPITI NGSAKHNISN VLQALAAAHS QGISLHELRK KAKSFIPDSV
LSQGRFNYQE IRGRKVLVDY AHNTAGLKAI FDTIAVFDKK RVISVIAGPG DRKDEDLKKM
AKITADHSDI FIIKEDDDLR GRKPFEVASI LKETALECSM EEHQTLIVPK ELEAFKKAWE
ISVPGDLLLL FYTDFAYVKE FLQGTMKQSS YKR
//
