ID B1V5E2_CLOPF Unreviewed; 874 AA.
AC B1V5E2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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:EDT70979.1};
GN ORFNames=CJD_2812 {ECO:0000313|EMBL:EDT70979.1};
OS Clostridium perfringens D str. JGS1721.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT70979.1, ECO:0000313|Proteomes:UP000003188};
RN [1] {ECO:0000313|EMBL:EDT70979.1, ECO:0000313|Proteomes:UP000003188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA Paulsen I., Sebastian Y.;
RL Submitted (MAR-2008) 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 -!- 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:EDT70979.1}.
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DR EMBL; ABOO01000032; EDT70979.1; -; Genomic_DNA.
DR RefSeq; WP_003475612.1; NZ_ABOO01000032.1.
DR AlphaFoldDB; B1V5E2; -.
DR Proteomes; UP000003188; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; 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; 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; IPR018109; Folylpolyglutamate_synth_CS.
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; 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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EDT70979.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 218..475
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 874 AA; 97853 MW; 9C0E1EDAB47CA762 CRC64;
MKINNQRIFE GRNIYSHRKC IRLDVDLEGY CETPTKDIDG FNERLLSYVP ELYTHRCGID
IEGGFVQRLK EGTYLAHVCE HTIIGIHNKL GIDIKYGKAR EIKDDFYYII FEYKLKRTAI
LIAELAIDLI NSIIKKKDIN FDERIEIIKR VIMEESIGPS TKAICDAAKE VGLPIITVGN
ENLYQIGYGK AGKRFSATIG NNTKGIAIDI ACDKMLTKEL LDIQNLPVAR GEKVFNTIHL
LEVVNRIGYP VVLKPQWGSK GNGVFVNINS EKELLRAYAE ITKECKEIMI EEYKVGNDYR
VMLVDYKVVA VSLRKPPYIT GDGVRNIRDL IEAMNANPLR GEGHEKPLTK VKIDEELINR
LSKLGYSLNS VLEYGEKVTL RGNANLSTGG SAEDYTDLIC KENIEICERA AKTIGLDICG
IDICAKSIAE PLYENDGIIL EVNAAPGIRM HHFPTIGKER NVGRKILDNM FKENYSNIPV
ISVTGTNGKT TTVRLISYVL NLIGFNVGCT TTSGVKIGNK YIHKGDDTGY NSARSVLLNP
EVDIAVLESA RGGLVRRGLA YDLADVGVIT NIREDHLGID GINDMEDLSF VKSLVGEAVK
DNGYSVINAD DEWSLKVLDR IKKPKILFSM NENNKYLQEN LKLGNPIVFY RDETIYVKNR
GKEYKIASAE EMKFTMNGKL KHNIENAMAA CAALVGIEVD YCIISKGLKQ FKSCEEDNRG
RFNMFDVNGV NVILDYGHNI DGYKVVIDSL KNLGLKNITG IIGVPGDRDL NTMKEVGRIS
GDFFDSIVIK EDKDLRGKDK GEVASIINEG VLSSNRKDLN VKIILSEEEA LRETLKLAKK
GETIIMFFED YESLYDIINE FKNKGTKDLK SASI
//
