ID A7G9M3_CLOBL Unreviewed; 873 AA.
AC A7G9M3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
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:ABS42519.1};
GN OrderedLocusNames=CLI_0175 {ECO:0000313|EMBL:ABS42519.1};
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS42519.1, ECO:0000313|Proteomes:UP000002410};
RN [1] {ECO:0000313|Proteomes:UP000002410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F
RC {ECO:0000313|Proteomes:UP000002410};
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000728; ABS42519.1; -; Genomic_DNA.
DR RefSeq; WP_011987221.1; NC_009699.1.
DR AlphaFoldDB; A7G9M3; -.
DR KEGG; cbf:CLI_0175; -.
DR HOGENOM; CLU_016806_0_0_9; -.
DR Proteomes; UP000002410; Chromosome.
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; 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; 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; 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.
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:ABS42519.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 218..470
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 873 AA; 97554 MW; F75B9487E3047ADF CRC64;
MKIENIRVFE GRNIYSHKKC IRMDVDLEGY SNISSKEIQE FNKTLLNYVP ELREHCCCVG
KKGGFVERLY EGTYLSHICE HVIIALQNRI GIDVSYGKAR EIEGEKYYII YQYKYKNMAI
ECGKIAVDLI NNIINGKRYN IKTKTRELVC LLKTEELGPS TLSIIQEAKK RNIPVTKIGE
DSMFQLGYGI KGETIEATIC NSTSAVSVDI ACDKLLSKNI LMDQCIPVAE GYKVKNYIDL
LFKAEKLGYP VVLKPRFGNQ GKGVVVNIKN QKELVNAYSI VNKKFQDIMI EKYINGKDYR
ACVVDGKVVA VAQRIPPYII GNGKSTIYEL IKELNRDERR GDGHEKPLTK VKIDKDLKNN
INKEGYTLGY ILPEGYKLEL RHNANLSTGG VAIDCTDLIC TETREVCERV AKAIGLNICG
IDICCSDISK PLKENEGIME VNAAPGIRMH QYPYKGKSRN VAKAIVDMMF KEYDGNIPII
SITGTNGKTT TTRLIAHILS FSGKKVGMTT TGGIYINNKC INKGDTTGYY SAKTVLTNKE
VEVAVLELAR GGLIRDGLPY DLADVGIITN VTEDHLGLGG INTLEDMAYV KALVGEAVKK
DGYVVINADD EASISIINRI KSKIILFTKN KNNPIISQYL DNKNLVLYLD EDTIYLKKLN
KNEEIINVNK IPITLGGKLI YNVENAMAAI AALIALGLDV NTIRQGLESF SNEEQNPGRF
NMYNVHGTNV ILDYGHNIEG YKVVLESIKK INHKRIIGVV GVPGDRTNSS TLKVGNICGE
NFDYVYIKED RDKRGRKHGE IADLLKKGIL ETGFKNSKLN IILDEEEALK KAIEFSNPGD
LVIMFFEEFE PAENIVKDKI KKGKITKRET ALA
//
