ID   C0Q8U5_DESAH            Unreviewed;       332 AA.
AC   C0Q8U5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=DdlB2 {ECO:0000313|EMBL:ACN14435.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:ACN14435.1};
GN   Name=ddlB2 {ECO:0000313|EMBL:ACN14435.1};
GN   OrderedLocusNames=HRM2_13240 {ECO:0000313|EMBL:ACN14435.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14435.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN14435.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP001087; ACN14435.1; -; Genomic_DNA.
DR   RefSeq; WP_015903222.1; NC_012108.1.
DR   AlphaFoldDB; C0Q8U5; -.
DR   STRING; 177437.HRM2_13240; -.
DR   KEGG; dat:HRM2_13240; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_1_7; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000000442; 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; 3.40.50.20; -; 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   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 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:ACN14435.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT   DOMAIN          113..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   332 AA;  36753 MW;  EDC71F94E221DA6A CRC64;
     MIIGITYDLR QDYLDMGYTE LETAEFDSVE TIEAIETTLQ GLGHETRRIG NAIRLTERLV
     QGERWDLVFN IAEGLHGIGR EAQIPAILDL YNIPYTFSDP MVMAVTLHKG MTKHIIRDAG
     LATADFKVAN SARDAWNLPF DPPFFVKPVA EGTGMGITAK SLVKNALDLP GVCQELVEQF
     HQPVLIEEFL TGREFTVGIV GTGTRAQVMG TMEIIVISSK KDEVYSFENK EGWKSKVQYL
     PLSPGTDPLI QAVEDLALSA WKVLGCRDGG RIDIRCDAAG RPSFIEVNPL AGLRPEYSDL
     PIVCQFFGTS YVQLIELILE SAMERVPVLE TA
//