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Database: UniProt
Entry: K9V4Z5_9CYAN
LinkDB: K9V4Z5_9CYAN
Original site: K9V4Z5_9CYAN 
ID   K9V4Z5_9CYAN            Unreviewed;       345 AA.
AC   K9V4Z5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:AFZ02502.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:AFZ02502.1};
GN   ORFNames=Cal6303_3577 {ECO:0000313|EMBL:AFZ02502.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ02502.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ02502.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ02502.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP003610; AFZ02502.1; -; Genomic_DNA.
DR   RefSeq; WP_015199129.1; NC_019751.1.
DR   AlphaFoldDB; K9V4Z5; -.
DR   STRING; 1170562.Cal6303_3577; -.
DR   KEGG; calt:Cal6303_3577; -.
DR   PATRIC; fig|1170562.3.peg.3897; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_796548_0_0_3; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000010477; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
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   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:AFZ02502.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT   DOMAIN          128..336
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   345 AA;  38158 MW;  2AE81EC2015D03F8 CRC64;
     MSVLRVLHLV GSAVDEFYCD LSRLYAQDCL DSTANTELYE FHIAYISPGG TWRFPRDLSS
     DAIASAEKVS LSGAIQILIS LKIDVMLPQM FCVPGMTFYR GLFDLLKIPY IGNTPDVMAL
     AANKAKTKAV VAFSGVSVPQ GELLHRGDSP HVTTPAVVKP VDGDNSLGVV LVKNPSDYES
     ALKTAFTHSS EVLVETFIEL GREVRCGVIV QDNQLVCLPL EEYQMDKEQQ PIRSYDDKLK
     RNEKGDLSAV AKGNTKSWIV DPSDPITQRV WDVAKKCHIA LGCQHYSLFD FRIDPTGKPW
     FLEAGLYCSF AQISVIPTMA KTSGISLEKL FHIMLNNLLV YSISN
//
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