ID   D0MCT3_RHOM4            Unreviewed;       336 AA.
AC   D0MCT3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ACY47043.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:ACY47043.1};
GN   OrderedLocusNames=Rmar_0135 {ECO:0000313|EMBL:ACY47043.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY47043.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY47043.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP001807; ACY47043.1; -; Genomic_DNA.
DR   RefSeq; WP_012842655.1; NC_013501.1.
DR   AlphaFoldDB; D0MCT3; -.
DR   STRING; 518766.Rmar_0135; -.
DR   KEGG; rmr:Rmar_0135; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_1_10; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000002221; 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:ACY47043.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   DOMAIN          119..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   336 AA;  37128 MW;  77C050818A9843E9 CRC64;
     MHPNGLMRIG IVYDLFDDYP WEVGEPPDAD AENEPPETVD VLAAAIRKLG HKPVRIGTAY
     DLLVELPDLR IDCGISIAEG ARGRNREAYA PMLFEMAGIP YIGSDPLTLS LSLDKAWTKD
     LVAAAGVPTP PYRTYAGPED VDPHDLPGPF PLFVKPRYEG SSKGITAASK VHSLEALREQ
     VARLTATYRQ EVIVEPFIEG SEFTVAVIGN NPPEPLPVLQ RAVEATTGIG LHALEHRGMK
     PAAALEAAPY VPLTDELERC LQQLAVRVYE KLQCRDFARL DFRVDREGKP WFLEINPLPT
     FAPDGTFAIL AELMQRPYVE FLAEILQRGL RRLGLA
//