ID   A9GAW9_SORC5            Unreviewed;       378 AA.
AC   A9GAW9;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=D-alanine--D-alanine ligase A {ECO:0000313|EMBL:CAN92922.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:CAN92922.1};
GN   OrderedLocusNames=sce2763 {ECO:0000313|EMBL:CAN92922.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN92922.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN92922.1, ECO:0000313|Proteomes:UP000002139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; AM746676; CAN92922.1; -; Genomic_DNA.
DR   RefSeq; WP_012235395.1; NC_010162.1.
DR   AlphaFoldDB; A9GAW9; -.
DR   STRING; 448385.sce2763; -.
DR   KEGG; scl:sce2763; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_7; -.
DR   BioCyc; SCEL448385:SCE_RS14165-MONOMER; -.
DR   Proteomes; UP000002139; 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; 3.30.1490.20; 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:CAN92922.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT   DOMAIN          128..336
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   378 AA;  40776 MW;  9CE59F4E41FEC06E CRC64;
     MPEPRILILS NRDPEEVVDE PPLAQRVGSG RLRLGREDGS AVVAESVLAA LAAAPGVRVA
     HRPVLRPSEV LAAIGDHRPD VIFNLCEALD GDSRHEVMCA WLLAGLDLRF TGSDHVALRS
     CLHKTEANRI LARAGVRVPA TVRVEGPDRI PEVAFPVIVK PEREDGSMGI DRGSVVHDRR
     ALRDQVAAVV AQCRQPVVVQ RYVHGREISV SLLGWPTPRV LPPGEVTFQG LPEGHPHVVT
     YESKWRPETA ASIGTPSSAA VLRPLELRRV VAVGRRAFEV LGLRDYGRVD VRLDERGTPH
     VIDVNPNCDL SPDAGFARAA ARAGLSYADV VWEILRAALA RGARHDDLLR ARGRAPARGR
     AAARSAARGA LSAAPEAP
//