ID   M0LSA3_9EURY            Unreviewed;       393 AA.
AC   M0LSA3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=C447_14321 {ECO:0000313|EMBL:EMA36442.1};
OS   Halococcus hamelinensis 100A6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA36442.1, ECO:0000313|Proteomes:UP000011566};
RN   [1] {ECO:0000313|EMBL:EMA36442.1, ECO:0000313|Proteomes:UP000011566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100A6 {ECO:0000313|EMBL:EMA36442.1,
RC   ECO:0000313|Proteomes:UP000011566};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA36442.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOMB01000041; EMA36442.1; -; Genomic_DNA.
DR   RefSeq; WP_007695088.1; NZ_AOMB01000041.1.
DR   AlphaFoldDB; M0LSA3; -.
DR   PATRIC; fig|1132509.6.peg.3342; -.
DR   eggNOG; arCOG06897; Archaea.
DR   OrthoDB; 11959at2157; -.
DR   Proteomes; UP000011566; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF15632; ATPgrasp_Ter; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011566}.
FT   DOMAIN          121..305
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   393 AA;  42758 MW;  44E406AF1841EA56 CRC64;
     MTEGRVLVLD AERRQAVVAI RSLGSAGVDV TAASGLRVNT GAASKHADRC VRYPRPRTDR
     GGFVDRIERE VREREYDMVL PMADPTVVPV VEARGRLEPH VRVPFPDAET LRIGTDKKRT
     VEAARAAGVP HPKTLVSEEL DLEAVESEVG YPVVLKPRMG AGRVGVSVCD NPAELEAAYA
     NADDRHRPLL VQEFIPNGGE RGVYTLYNHS SELRAVTVQQ RLRTDPPEGG TSSLRETVAD
     PELVSSTDEF LSGLGWQGVA MAEFRVDPRD GEAKLLEINP RLWGSLALTV AAGADIPVLL
     HRLATEGDCE TSLDYQVGVQ ARHLLGDVSN LLASADKRSA LRAFLRPADG PRYHDVLSTD
     DPGATALYFL SEVGKFASRR LPRLRRPTTD AGP
//