ID   E1QG75_DESB2            Unreviewed;       340 AA.
AC   E1QG75;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:ADK83587.1};
GN   OrderedLocusNames=Deba_0210 {ECO:0000313|EMBL:ADK83587.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83587.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK83587.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP002085; ADK83587.1; -; Genomic_DNA.
DR   RefSeq; WP_013257043.1; NC_014365.1.
DR   AlphaFoldDB; E1QG75; -.
DR   STRING; 644282.Deba_0210; -.
DR   KEGG; dbr:Deba_0210; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_7; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
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:ADK83587.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT   DOMAIN          109..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   340 AA;  37568 MW;  9754DAC7F76796F8 CRC64;
     MKVVVLHDMA SPDAAPDLAD NVVQASQVLA ALGRLGHRAQ GLAFGPEVDQ TRQALEELRP
     DVVFNLVETP LGMARMIHLA PLLLERLRLR YTGAGARGML LTSQKLLAKK AMRESNLPTP
     DWCGPRDDGL PFSPLRRYIV KSVWEHGSVG LDDHSIIKPL GRAAMRAAIA QRGKALGGDC
     FAEAYIDGRE FNIAILAGSR GPEVLPPAEI TFEGFQPGKP HIVGYRAKWV EDSHEYNHTP
     RRFDFEPRDA ELLARLKAMS LRCWRLFGLR GWARVDFRVD RKGRPFILEV NANPCLADDA
     GFMAAARRAG LDQTIVVWRI LGSASRGRRR GCAVEKTGLA
//