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Database: UniProt
Entry: A0A1F8NV33_9CHLR
LinkDB: A0A1F8NV33_9CHLR
Original site: A0A1F8NV33_9CHLR 
ID   A0A1F8NV33_9CHLR        Unreviewed;       360 AA.
AC   A0A1F8NV33;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=A2Y93_08210 {ECO:0000313|EMBL:OGO14760.1};
OS   Chloroflexi bacterium RBG_13_68_17.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797638 {ECO:0000313|EMBL:OGO14760.1, ECO:0000313|Proteomes:UP000178211};
RN   [1] {ECO:0000313|EMBL:OGO14760.1, ECO:0000313|Proteomes:UP000178211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO14760.1}.
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DR   EMBL; MGNF01000063; OGO14760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8NV33; -.
DR   Proteomes; UP000178211; 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; 3.30.1490.20; 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   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   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          118..326
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   360 AA;  40102 MW;  9515C117FD051513 CRC64;
     MSAYNDRTDL PVLLLHNLDL TWSPSDREEA EQQASKLKTA LRDLGHPVAS VPVVDANLAP
     RLRDYDPRDY IVFNWCEGLP GIPRSESRVA RTLAAMHFAY TGSTSRVLDL SWDKPRVNTL
     LDRRGIPSPR WRVFETAQTG EWDCFPAIVK PAYEHCSYGV TSGAVVLDPD ELRGRVQYVL
     DTFGEPALVE DFIDGREFHV GVWGDGQLEM LPPAEMDFAF FEDVRDRLCT YDAKFTPGTP
     HYDQIQLRLP APLTDEELAA LQRTVFATYR ATGCRDYARF DVRLRDGIFY ILDINPNADI
     SSEASLACAA EVAGYTFGRM ASRLVNLAAR RHPVFGAAPP AGPFASLLHP TGQISPIPAS
//
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