ID A0A1T4N5H7_9FIRM Unreviewed; 880 AA.
AC A0A1T4N5H7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN02745118_01706 {ECO:0000313|EMBL:SJZ74610.1};
OS Selenihalanaerobacter shriftii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Selenihalanaerobacter.
OX NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ74610.1, ECO:0000313|Proteomes:UP000190625};
RN [1] {ECO:0000313|Proteomes:UP000190625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUWM01000013; SJZ74610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4N5H7; -.
DR STRING; 142842.SAMN02745118_01706; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000190625; 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: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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190625}.
FT DOMAIN 220..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 880 AA; 96375 MW; 01F11EDD9348FC9E CRC64;
MRLIEISKLI GPNIYTYYPA IRVKLDLEDL DKVESKEVER FNSKLITLIP TLKEHYCALG
QPGGFLIRLK EGTYFGHVVE HVAIELLNLI GHKVNYGCTR ESEVSGIYNI IYEYQSYAPA
ILAGKEAYKI VKSIINGQEV SMEEIIEGLN KEDVKASLGP STQAIVDAAH KRNIPTIRLG
KRNSLVQLGY GIEQKRIQAT ISQITSCVGV DIACNKNLAK ELLKDMGVPV AKGDMATTEK
EALEIARNLE GKIVTKPYNS NQGKGISLNI KTDYDVMNGF KLAQSYSQEV MVEKMISGND
YRVLVINGEV VAVAQRIPAH IVGDGEATIL ELIQEVNKDP LRGEGHSSPL TRIRVDEAVL
FLLAKQDYHL DSVISRGEQV FLRETGNLST GGTAIDKTDE IHPVNKQLAI RAAKVIGLDI
AGIDLITPDI SQPLNNGRGA IIEVNAAPGI RMHHYPTIGK SHDVAGAIVD MLFPAGNSGR
IPIISITGTN GKTTVTRLVS LILQQADYQV GMTTTDGIYI NQKRLLKGDT TGPISAQFVL
KDSDVEVAVL ETARGGILRA GLGYDESDIG VITNISSDHL GQGGVEDLED LADVKSLVIE
RVNDEGTAIL NADDQEVVKL SSRSNVQNII YISSQENNFI LRKHLAQGGT GIYVKDNRII
INHNQKEIEV EDIREIPATY KGIAKHMVEN ILFATAIAFD FGIDVKLIKN VLNNFGGNHQ
QNLGRLNIVE IAGVKVILDY GHNLAGYQAT LEVARELEAE KVIGVIGVPG DRKDESILEI
GKISGEYLQK VIIKEDQDLR GRKEGEVAEL LASGVNNAED KLEIEIVLSE IEAVKQALNE
IEPGQLLIIF YEKDPAGLLD LIQTELKLKE KKLAEILVTE
//
