ID A0A0J1FF54_9FIRM Unreviewed; 881 AA.
AC A0A0J1FF54;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:KLU62062.1};
GN ORFNames=CEB3_c15810 {ECO:0000313|EMBL:KLU62062.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU62062.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU62062.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU62062.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) 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:KLU62062.1}.
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DR EMBL; LDXJ01000049; KLU62062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FF54; -.
DR STRING; 999898.CEB3_c15810; -.
DR PATRIC; fig|999898.3.peg.1799; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000035957; 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; 3.30.470.20; 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:KLU62062.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000035957}.
FT DOMAIN 220..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 881 AA; 95189 MW; 76928F264B835173 CRC64;
MEIKQIQAIE GANVYSHRPV IRAILDLREW ADKTSDRLGD FNDRLVAYLP GLSEHHCSRG
KPGGFLERLA EGTLIGHVTE HVTIELLTRA GQDISYGKTM SLPERPGVYE IIFNYQSKEG
GIEAFRQAVV LVDSLLSGKE FNTREIVNKL RKVIAENDLG LSTKMIIKAC QERGIPFRRL
NEYSLLQLGY GRNQRRLQAA MTDRTGCIGV DIAGDKGLTK RLLKAAGIPV PFGLVAKEES
EAAAALQVIG GPVVVKPYNG NQGKGVSLKL TSEGEVRTAF RVAQIYGSDV IVEEFIEGHH
YRLLVVGGQL AAASERIPAH VVGNGRATIA ELVEQTNANP LRGEDHEKAL TKIRIDPVVI
LTLAQKKLTM DTVPAAGEIV YLRDGANLST GGIALDVTDS VHPDNVDLAV YAAKVVGLDI
AGVDIVSSDI AASYRKANGR VIEINAAPGI RMHHYPSVGQ AKDVGKAIVN LVLPTGNGRI
PIVAVTGTNG KTTTTRMIGK MLLDQKLSVG MATTDGIYVQ GKLLVEGDTT GPESARTVLS
HPEVQVAVLE TARGGILRAG LAYDYADVAV ITNISADHLG QYGIEDLDDL TRVKSLVAEV
VKPHSYVVLN ADDPYVLKMA GRTNGKVILF SQHKDNIHVR KHLGRGGGAV FVRRGVILYC
QGSQSYRICG VRQLPITLGG RARHNAENAL AAVAAAWALG LSAESIRQSL GNFLPDGQNS
RGRLNFYEIG GVNVWVDYGH NAAGVREIIQ TLKKCKAGSS FVGCVTVPGD RTDAEIKELA
RVAAQGFQRL IIKEDEDLRG RQPGEIAAII RAEAIRAGMP ANRLTTVLNE REAFSYGLDS
CLPGEVFVMF YEHLDPIEEE IRRRLRLEEG SSGRAVGEAG K
//
