ID L0ILE3_THETR Unreviewed; 875 AA.
AC L0ILE3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Thethe_02760 {ECO:0000313|EMBL:AGB20315.1};
OS Thermoanaerobacterium thermosaccharolyticum M0795.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=698948 {ECO:0000313|EMBL:AGB20315.1, ECO:0000313|Proteomes:UP000010845};
RN [1] {ECO:0000313|EMBL:AGB20315.1, ECO:0000313|Proteomes:UP000010845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0795 {ECO:0000313|EMBL:AGB20315.1,
RC ECO:0000313|Proteomes:UP000010845};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Feinberg L., Folden J., Hogsett D.,
RA Shaw J., Woyke T.;
RT "Complete sequence of chromosome of Thermoanaerobacterium
RT thermosaccharolyticum M0795.";
RL Submitted (MAR-2012) 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; CP003066; AGB20315.1; -; Genomic_DNA.
DR RefSeq; WP_015312718.1; NC_019970.1.
DR AlphaFoldDB; L0ILE3; -.
DR KEGG; tto:Thethe_02760; -.
DR PATRIC; fig|698948.3.peg.2752; -.
DR HOGENOM; CLU_016806_0_0_9; -.
DR Proteomes; UP000010845; 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; 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};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 217..470
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 875 AA; 96638 MW; 24369C266A6AB1B7 CRC64;
MIIKDIRVYR GRNIYCHRPV VKMIVDTGDY DIPTKDIPGF NERLIKTIPS LNKHCCSYGY
EGGFLKRLDE GTYLPHVTEH IILEIQNILG YDVKYGKARL IEGHLYNVIF EYELEECAIR
SAKLAVKMVN KFISGEDFDF EQELEQIRKV VVEVELGPST MALKKAAEEA SIPVTRVGNG
SILRLGYGRY QKMIEGTITQ NTSCIAVDIA CDKILTKNII KEYGLPVPEG DVAYNENDAI
GIAEEIGYPV VVKPFNGNQG KGVFLNLLNK EELIVAYRNA KNISDLVIVE RHIKGKNYRV
LVVGDRVVAV SERIPARVLS DGIHTIRELV EIENRNPLRG VGHEKPLTKI NIDNISQFVL
KKQGYQIDDI PPKGVYVYFR ESANLSTGGT AIDRTKEIHP DNIEIAVRAA KAIGLDIAGI
DITMENISMP LNRSNGAIIE VNAAPGIRMH HYPSKGKSRD VAKAIVNMLY PKGSKATIPI
ISVTGTNGKT TTVRMISQIL RMYGYTVGMT STDGIYVDDV CIYKGDNSGP KSARTCLADK
NIDAAVLETA RGGIVREGLG YDLADVGIIT NISEDHLGID GIETLEDLAF VKSLVVEAVK
KDGYSVLNAD DPMTPYISKR AKGKIIYFSM HENNITIKRH LEEGGISVYV KNDTIVIANG
EIVPVAKIDE IPATLNGKVL YNVENAMAAI AASYGIKIPV NVISKGIKSF YCDENHNPGR
FNIFNVGSFR VLVDYGHNID SIRKVIESAR KLNPNRLLGV IGVPGDRSDS STLKIGEICG
EGFDKVYIKE DLDLRGRKPG EIAKLLEIGV LKGGLSKEDV NVILKEVDAL KTAMYEAQPG
DLIVIFYEKY APVVDAINNF IKISQFDIDE SKERA
//
