ID A0A0S8GPW3_9BACT Unreviewed; 325 AA.
AC A0A0S8GPW3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=AMJ79_14930 {ECO:0000313|EMBL:KPK73869.1};
OS Phycisphaerae bacterium SM23_30.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK73869.1, ECO:0000313|Proteomes:UP000051901};
RN [1] {ECO:0000313|EMBL:KPK73869.1, ECO:0000313|Proteomes:UP000051901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK73869.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK73869.1}.
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DR EMBL; LJUC01000249; KPK73869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8GPW3; -.
DR STRING; 1703411.AMJ79_14930; -.
DR Proteomes; UP000051901; 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: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 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 103..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 325 AA; 37241 MW; B79688634CBA0406 CRC64;
MISDDDPQFT RSTEEALTEY HVVDTLRTLG HEVSVQGAVG DLPALVSSLT EEAPDLVFNL
TEQYGGDRRL DKNITALLEL LDLPYTGTGS MGLLLCRDKR LCKQLLSLHK IRVPQFISLP
TGRSLQVPRK LPYPLVVKPA FEDGSEGISN ASLVYNENAL RERAAFVHDR WDQAAIAEEY
IEGQELYVSL MGNKRLTVFP IRGCIFDYDG EEGPNLVTYR VKWNKEYQEK WNIRFAFIPF
ELDIVRKIER ICKKVYRVLQ LRDYGRIDVR LTPDNKLVVL EANPNPDIAY GDEVAEAAEK
FGLSYENLID RILRNALRRY EQRAK
//
