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Database: UniProt
Entry: D5SQN3_PLAL2
LinkDB: D5SQN3_PLAL2
Original site: D5SQN3_PLAL2 
ID   D5SQN3_PLAL2            Unreviewed;       871 AA.
AC   D5SQN3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Cyanophycin synthetase {ECO:0000313|EMBL:ADG68495.1};
GN   OrderedLocusNames=Plim_2672 {ECO:0000313|EMBL:ADG68495.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68495.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG68495.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
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DR   EMBL; CP001744; ADG68495.1; -; Genomic_DNA.
DR   RefSeq; WP_013110926.1; NC_014148.1.
DR   AlphaFoldDB; D5SQN3; -.
DR   STRING; 521674.Plim_2672; -.
DR   KEGG; plm:Plim_2672; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_016806_0_0_0; -.
DR   OrthoDB; 9803907at2; -.
DR   Proteomes; UP000002220; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR011810; Cya_phycin_syn.
DR   InterPro; IPR044019; Cyanophycin_syn_N.
DR   InterPro; IPR036565; Mur-like_cat_sf.
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; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF18921; Cyanophycin_syn; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002220}.
FT   DOMAIN          219..469
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   871 AA;  93892 MW;  C383229B5A79A1EC CRC64;
     MQIRSVRALR GPNIWSRQPC LEALVDLGPL KDLSSELIPG FNDRLMSWLP GMIEHRCSVG
     ERGGFFVRLR RGTYLAHILE HVTLELQTMA GTNVGFGRAR ETSEEGVYKV AIRYAEESVG
     RAALEVAHRL CLAAVYDQPF DIQAETIRLR ELADRVCLGP STQAIVSAAL ARNIPYRRLN
     TGSLVQLGQG FRQRRIWTAE TDSTSAIAES IAQDKDLTKS MLRAAGVPVP EGREVKDPGD
     AWEASQEIEG PIVVKPIDAN HGRGVCMNLE TEEEIRDAFV VASQEGSGVI VERFAPGSEH
     RLLVVGDRLV AASRGDAAKI EGDGEHNVAE LIQRQVNSDP RRGDDEIFPL STVRLDDGVV
     LLELKRQGYT PESIPPAGAV VIVRRNDNLS IDVTDEVHPR NAEHAVMAAR IVGLDIAGVD
     IVTEDISQPL EEQGGAIVEV NAGPGLLMHL RPAVGKPRPV GEAILERLFP PGTSGRIPLV
     CVTGVNGKTT TSRLVASILR QAGIKVGVAT SDGIVVEDRV IELGDCAGPK SARAVLLNPT
     VEAAVLEAGR GGILREGLGF DKCDVAVVTN LSEPDHLGEY DIHTVEKMYS VKRTPVDVVM
     PGGFAVLNAA DPWVAKMSTL SAGGVIFFAR DERQPVLSQH RSEGKKVVFV RDGWIVAGDG
     GLSSQIVRLA DVPCTHGGRI GFQIDNVLAA TAAAWGLKIP FSAIAAGLQH FQGNLADDPG
     RFNVFQLGGK TLIVVDARNP SALKATIAGL EAFSSQRKLV VYAAENDRIH SDITQQGELL
     AEHFQNFYLY HLPGCATTGA DAPRELLLAS IRATADSEKL CVNLEEDWQK AVDAAWHDFR
     EGDVLLIQAG AISATIRKVQ QLLGLELVSK A
//
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