ID A0A1J4RQR9_9BACT Unreviewed; 332 AA.
AC A0A1J4RQR9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=AUJ59_00785 {ECO:0000313|EMBL:OIN89729.1};
OS Candidatus Beckwithbacteria bacterium CG1_02_47_37.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1805034 {ECO:0000313|EMBL:OIN89729.1, ECO:0000313|Proteomes:UP000183144};
RN [1] {ECO:0000313|EMBL:OIN89729.1, ECO:0000313|Proteomes:UP000183144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_47_37 {ECO:0000313|EMBL:OIN89729.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIN89729.1}.
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; MNUI01000017; OIN89729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4RQR9; -.
DR STRING; 1805034.AUJ59_00785; -.
DR Proteomes; UP000183144; 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 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; 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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 108..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 332 AA; 37519 MW; 8728D5EC1E26D69A CRC64;
MKLTVGFTYN LKRERGEIEF DSPEVISLIK KAIEQLGHKV ILIEADLNAY DRLKKLKGKV
DIVFNIAEGL GGSGREAQIP IFCEMLGIPY THSRPTVHAL GLDKTLTKKV IAGAGVPAPK
SLLITTFKAA AQINLGFPLI IKPNREGSSL GVFDKNVVEN KSQLYKRLRL MLRQFRPVMV
EEYIDGREFT VSLLGDQPEV LPILEQKFAF LPKGFHRIAG YELKWLYEDR LTDQAEAYAC
PAKLIRRQIQ TIKALSVKVF KALEVNDCAR IDWRMGRTGR FYFLEINTLP GLNFSGKEIS
YFPLSARAAG YDLTRVVDII LTSALRRFNL LK
//
