ID   D5ECQ3_AMICL            Unreviewed;       367 AA.
AC   D5ECQ3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ADE56335.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:ADE56335.1};
GN   OrderedLocusNames=Amico_0188 {ECO:0000313|EMBL:ADE56335.1};
OS   Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC   Aminobacterium.
OX   NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56335.1, ECO:0000313|Proteomes:UP000002366};
RN   [1] {ECO:0000313|EMBL:ADE56335.1, ECO:0000313|Proteomes:UP000002366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX   PubMed=21304712;
RA   Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT   1).";
RL   Stand. Genomic Sci. 2:280-289(2010).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP001997; ADE56335.1; -; Genomic_DNA.
DR   RefSeq; WP_013047601.1; NC_014011.1.
DR   AlphaFoldDB; D5ECQ3; -.
DR   STRING; 572547.Amico_0188; -.
DR   KEGG; aco:Amico_0188; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_1_0; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000002366; 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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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   InterPro; IPR016185; PreATP-grasp_dom_sf.
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   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000313|EMBL:ADE56335.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002366}.
FT   DOMAIN          134..344
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   367 AA;  41517 MW;  02D15E90D7BF5105 CRC64;
     MERRHEEERE NPLPLKKRKK EVQVIGITYN LRKDAQADEP DDIYEEYDCL ETVEALSNEI
     ASLGFQVFLF EQNELLLQKL DSIAPDFVLN IAEGLGNYRG RESQVPCILE SLNIPFSGSD
     SASLAIALDK VLTSHVLRAS NIPAPKNYVA KLPQDTTEKK VIFNTCQKYI IKPRWEGSSK
     GIFLDSIADT PEKVKTCIKR IWERYNQPAI VEEFLPGIEI TAGVAGNTQP KCIGMMSITP
     VTENSSFLYS LEEKRNYLER IRYSGPDSMS PQLRKKIGDL AVRAFKALEL RDIARIDFRL
     DDKGQPRVID INPLPGLSPA YSDLPILYRL SGGEYSELIQ TILREAFSRY GLCAPCLNKP
     ELVREKA
//