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Database: UniProt
Entry: A0A1F8PWY0_9CHLR
LinkDB: A0A1F8PWY0_9CHLR
Original site: A0A1F8PWY0_9CHLR 
ID   A0A1F8PWY0_9CHLR        Unreviewed;       353 AA.
AC   A0A1F8PWY0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=A2W33_00930 {ECO:0000313|EMBL:OGO27642.1};
OS   Chloroflexi bacterium RBG_16_52_11.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797646 {ECO:0000313|EMBL:OGO27642.1, ECO:0000313|Proteomes:UP000179327};
RN   [1] {ECO:0000313|EMBL:OGO27642.1, ECO:0000313|Proteomes:UP000179327}
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OGO27642.1}.
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DR   EMBL; MGNN01000050; OGO27642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8PWY0; -.
DR   Proteomes; UP000179327; 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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; 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; IPR000291; D-Ala_lig_Van_CS.
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; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          116..344
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   353 AA;  39385 MW;  D7690D02FD1575BA CRC64;
     MKKFRVALLA NLKANAPKFD GMAEDQWDDL DSEKTVNSLV TAIRAGGNYC EFFEGDITVI
     DNLAKYQPDI CFNICEGHFG DAREAQIPAL LEMLRIPYSG SKVMTLSLAL DKPMTKRVLA
     YHELPTPAFQ TFERVDEPLN DDMLFPLFVK PSREGTGMGV SGKSIVNNET ELREQVSYTH
     ERYKQPALVE RFISGREVTL GVVGNLIGPV ARRLPADEAA PRIQSGLRFF PPMEVNLQPF
     EDSDIVYSNR LKVDLADQLD YICPAPLDDD MVDELNWLTA AVFRITGALD VSRVDFRLDA
     EDNWKPSILE INPLPGLSPG VSDLVIEAAA EGVDHTYLVN MILDTALKRY GLI
//
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