ID B2TJL9_CLOBB Unreviewed; 872 AA.
AC B2TJL9;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
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:ACD22120.1};
GN OrderedLocusNames=CLL_A0470 {ECO:0000313|EMBL:ACD22120.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22120.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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}.
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DR EMBL; CP001056; ACD22120.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TJL9; -.
DR KEGG; cbk:CLL_A0470; -.
DR HOGENOM; CLU_016806_0_0_9; -.
DR Proteomes; UP000001195; 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; 3.30.470.20; 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; 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:ACD22120.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 218..471
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 872 AA; 97403 MW; 6BDCC626EA8BD66E CRC64;
MKVVQERIYE GKNIYSHKKC IRMDVDLQGY CETPSKDIPN FNFNLLKLVP ELYTHRCGID
EEGGFVTRLK EGTYLAHICE HITIALQNRL GIEVAYGKAR EIQGDRYYII FQYEYAKTAM
ECFKLSMDLI NALITQSPIN FEERINSIKE ILNLDEIGPS TNAICKAAKE YNMPITQLGN
SGFYQIGYGK QGKVIEAAIS EKTSCVAVDI SCDKFLTKQL LANQNIPVAL GGKVYNIIDL
LKCAEKIEYP VVLKPQYGSK GNGIYLNIKN ENELIKSYNN LKNKFKDILI EKYIEGNDYR
VCVIDYKVVA VSLRIPPFVI GNGKETLKEL IENINKDPLR GEDHEKPLTK IKIDDQLISY
VNKNNLSLSY IPKDNEKVFL RENANISTGG IAIDCTDNIC EENINHCINA AKALGLDICG
IDLCVDDISC DIAKSNGVIM EVNAAPGIRM HHFPSKGIER NVGKAIINMM YGENPKNIPI
VSVTGTNGKT TTTRLINHVL SQMGYSVGMT STEGIYVNNK CIHKGDDSGF NSAKTILLNR
DVDIAVLETA RGGLIRKGLA YDIADVSVIT NITNDHLGLD GINSMEELSF VKALVGEAVK
ENGFTILNAD DEWSKTIINR IKANKIFFSK YADNELIQKN IIDGGISVFI ENDNIIVVNN
HKKYSICSIN DVPLSYNGLL KYNLENIMAA CGALVGMNID YCMISKGIMS FNLNNNNGRF
NIYEIEDRKI ILDYGHNIEG YKAVLSSLDK IKKDKDLIGV IGIPGDRCDD IAIEIGEICS
EMLDKIIIKE DKDRRGRDEG EIASLLKNGV LRKNKNAKIH VCLDEIKALE KALMISKKGD
TIVVFFEDLE SIVKYINNKN LNNSLNLKLS NL
//
