ID A0A1F8PHX4_9CHLR Unreviewed; 362 AA.
AC A0A1F8PHX4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=A2Z28_04280 {ECO:0000313|EMBL:OGO22722.1};
OS Chloroflexi bacterium RBG_16_51_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797645 {ECO:0000313|EMBL:OGO22722.1, ECO:0000313|Proteomes:UP000179905};
RN [1] {ECO:0000313|EMBL:OGO22722.1, ECO:0000313|Proteomes:UP000179905}
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:OGO22722.1}.
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DR EMBL; MGNM01000072; OGO22722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PHX4; -.
DR Proteomes; UP000179905; 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: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 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 117..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 331..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 39664 MW; B604EE805374FDEE CRC64;
MRKHIAIVYN KPEPSRYDAT GEVKAALGVV DAVQAVEQSL LELDYSVKLL PLTFPFEAER
EKLKFRDFDL VFNLFEGFCG YPETEALVPE ALDELGIPYT GCRGNILRLA LDKAKVKVFL
QAAGIPTPDA QLLTPQTLDL FQLSFPCIVK PSGEDASHGL TGDSVVSDFA SLERQVRVIS
ESYGGRALVE KFLSGREYSA TVMGKSQYSV LPVSEMVYAL PPGMARILTF EAKWEPGSPY
YQGTTTVCPA EIEVEEQERI ANTALSVFRV IGCKGYGRVD MRADSEGLIN VIEVNPNPDI
SPGTGVARQT AAASMTYTEF VERIIEIALE KEPDDNQHPS NAEARQASLD ANPAEYPRVQ
AG
//
