ID   A0A0G0C797_9BACT        Unreviewed;       811 AA.
AC   A0A0G0C797;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=UR30_C0011G0010 {ECO:0000313|EMBL:KKP39267.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP39267.1, ECO:0000313|Proteomes:UP000034765};
RN   [1] {ECO:0000313|EMBL:KKP39267.1, ECO:0000313|Proteomes:UP000034765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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:KKP39267.1}.
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DR   EMBL; LBOR01000011; KKP39267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0C797; -.
DR   STRING; 1619061.UR30_C0011G0010; -.
DR   Proteomes; UP000034765; Unassembled WGS sequence.
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; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR041472; BL00235/CARNS1_N.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR040570; LAL_C2.
DR   PANTHER; PTHR23132:SF14; ATP-GRASP DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          124..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          576..791
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   811 AA;  92996 MW;  80E8BD037F991F4D CRC64;
     MVFYNFPINF QEKTILLVNT GSIKKRFIIQ KLKKSGLKIV VLHKEKNWAQ SYVDHFIIAD
     TTHHNEALQA VLNFLSSHPE VKFDGVLTFW EDDVILTSRI ADRLNLIGIP YSVVKRVRNK
     YNFRDFCRKH NIYAPDHFLI KNVDDLQIVK KNLNFPIVLK PVYGSSSAFV VKVENKNNLD
     EMYNYLRTNI SPNIESALND GLDILAEEYI DGEEVDIDIL IQNGRIKFYS ISDNCKTKEP
     FFVETGGAIP SNLSDHDQHA LINMADETLE KLNIQNGCIH FEAKMSSKGP VPIEVNLRMG
     GDDVYNLVKR AWKVDLVENA LKIALGIYIP KIKKPEFPYK YLASKYFLPD HSGILSQYNI
     HPDLEKKKFI EEVNFYKKVG DSVMAPPYGY EYLGWINVSG DSRIEAIENL DEAYNLVKYE
     ISKFNQGSFI GKTLRKNAYS PTFLKSKSLV GYSKIERIRK MSIKDQRNLH VGIAGNLYAD
     GGDLIEKDLM NISKSIMNHL EERGYKVSFF DFSNWQQAIN DLKASNIDIV FNVCERINDS
     SLLEPHAASL LDIFQIPYTG SNPFTLSLCI DKIRVKKLLT YHNIPTPKWD YVYSLDDDIR
     NDLKYPLIVK PANTDNSIGI TNDSVVTNKK QLMRQLRIIV EDIGSPALIE EYISGDEYDV
     SILGSEEDDL RVLPLSRSIF KNLPKGYWHI YAQEAKFGPE HNVYNDNIIV QRPPKGLSSR
     LTSLITEIAL DTYNILDCHD YGRVEVKVDE NNNPYVLELN PNPSIDKVDC VSLVAKIAGM
     DYGDFLEEII RLAIKRYKNR PPYYHLQTNL I
//