GenomeNet

Database: UniProt
Entry: A0A1J0KW00_9GAMM
LinkDB: A0A1J0KW00_9GAMM
Original site: A0A1J0KW00_9GAMM 
ID   A0A1J0KW00_9GAMM        Unreviewed;       941 AA.
AC   A0A1J0KW00;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:APC97895.1};
GN   ORFNames=KX01_1033 {ECO:0000313|EMBL:APC97895.1};
OS   Francisella frigiditurris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=1542390 {ECO:0000313|EMBL:APC97895.1, ECO:0000313|Proteomes:UP000182521};
RN   [1] {ECO:0000313|Proteomes:UP000182521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CA97-1460 {ECO:0000313|Proteomes:UP000182521};
RA   Kuske C.R., Challacombe J.F., Daligault H.E., Davenport K.W., Johnson S.L.,
RA   Siddaramappa S., Petersen J.M.;
RL   Submitted (OCT-2014) 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   -!- 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; CP009654; APC97895.1; -; Genomic_DNA.
DR   RefSeq; WP_071663960.1; NZ_CP009654.1.
DR   AlphaFoldDB; A0A1J0KW00; -.
DR   STRING; 1542390.KX01_1033; -.
DR   KEGG; frc:KX01_1033; -.
DR   OrthoDB; 9803907at2; -.
DR   Proteomes; UP000182521; Chromosome.
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; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
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; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF18921; Cyanophycin_syn; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 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   Ligase {ECO:0000313|EMBL:APC97895.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          232..485
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   941 AA;  103565 MW;  EB443335C4D2EE4D CRC64;
     MKVLATNVYV GPNIYANFPV IRSEIDLGVL EEWPSAKIGT EFVDKLVENL PGLKEHGCSY
     REEGGFIRRL KEDEGTWMGH IWEHVILELQ SMAGSDVTFG RTRSTGEPGH YNMVYEYKQK
     DVGLRAMELA RELLLSILPQ QLQEEVGYKA DDFDFEYEKV KFIKFAQSKE FGPSTGSLVE
     AAKKRDIPYI RLNDQSLVQF GHGKYQQRIQ ATITSQTTNI AVQMSCDKEQ TNKILGALGL
     PVPQQKMVRT EADALRAAQK LGFPLVVKPL DGNHGRGISI NLKTYEEIRE AFVEASKVSR
     YVLVEQYATG FDHRMLVVNG KLVAVAKRVP GHVVGDGKST IEELVEIVNQ DPRRGIGHEK
     VLTILELDYQ ANTLMKAAGY NKDTILKEGE IFYLRSTANL STGGTAIDVT DIVHPDNRDM
     AERAIRAIGL DVGGVDFLID DIAQSYHEIG GAICECNAAP GFRMHVAPSE GQPRDVAGAV
     IDMLFPKELG NARIPIAAIT GTNGKTTTSR MVAHMWKNAG KVVGLTTTDG IYINGKLTVS
     GDTTGPASAQ MVLRDPTVEM AILETARGGL VRSGMGYDYC NVGACLNIAS DHLGLKGVNT
     LEDLAKVKSV VVEAAKDVAV LNADDPHCLK MSAKVTAKNI FYVTMNPEHA LVRQHIRAGG
     KAVVIEKGVN GDMITIFDNH IHIPVLWTHL IPATMEGKAI HNVQNSMFAI AISYSMGMSL
     DNIRDGLRTF VTSFYQAPGR MNWFEEHNFK VLMDYGHNPA AIKLVGHMIS NMDFTGKKIC
     VIASPGDRRN EDIHELAAAA APHFDYFICK RDDDLRGRKP EEVPEMLKAG LIKAGISAEN
     IEIIQDEVEA VNTALSMAEE GDLVTIFADK LKRTWKQIIY FNREDDEVEK GEVKTKTHEP
     FSASVIAQDP SLSKEISEVI KAGIISDGSG VRVASFDEDS D
//
DBGET integrated database retrieval system