ID A0A0R2PUP1_9MICO Unreviewed; 379 AA.
AC A0A0R2PUP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=ABR66_00525 {ECO:0000313|EMBL:KRO39789.1};
OS Microbacteriaceae bacterium BACL25 MAG-120322-bin65.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX NCBI_TaxID=1655574 {ECO:0000313|EMBL:KRO39789.1, ECO:0000313|Proteomes:UP000053725};
RN [1] {ECO:0000313|EMBL:KRO39789.1, ECO:0000313|Proteomes:UP000053725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL25 MAG-120322-bin65 {ECO:0000313|EMBL:KRO39789.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO39789.1}.
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DR EMBL; LIAY01000010; KRO39789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PUP1; -.
DR Proteomes; UP000053725; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR011127; Dala_Dala_lig_N.
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 Pfam; PF01820; Dala_Dala_lig_N; 1.
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 141..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 379 AA; 39504 MW; CDDC6DABE126B169 CRC64;
MSDSTWAVVF GGPSPEHEIS ILTGLQAERV LLDGGASVVA LYVSPTGGWY QVPSASEAGD
FLTGAPAGSK ELEVVISSQP GIYAKKGMGR KALEIDAALL CFHGGLGEGG GAAAVFNYLD
IPATGSSVFA GAVGMDKLAF GGLMGSEGIA SLPREALSHT REPSFAGPYI VKPRFGGSSI
GIEIVDDIAT ARTLAKTSPH LSVGAVLEPY RPHLVDLNIA FRTSPQLEFT DLERPLRTEG
ESTGLYSYQE KYLAGGSAGL THAPREFPAQ APRAVHDAAR VLATAVAEVT RLSGIVRVDL
LWDEKTGEVF VNEVNTIPGA LSLYLWAPKH PAFTVLIDAL EEARDKPVVF PQSGFGQGVA
LRAAGGIAGK LVGLDGPRG
//
