ID A0A6G9YF23_9NOCA Unreviewed; 325 AA.
AC A0A6G9YF23;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 02-APR-2025, entry version 13.
DE SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:QIS11730.1};
GN ORFNames=F5544_19310 {ECO:0000313|EMBL:QIS11730.1};
OS Nocardia arthritidis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Nocardiaceae; Nocardia.
OX NCBI_TaxID=228602 {ECO:0000313|EMBL:QIS11730.1, ECO:0000313|Proteomes:UP000503540};
RN [1] {ECO:0000313|EMBL:QIS11730.1, ECO:0000313|Proteomes:UP000503540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00012717 {ECO:0000313|EMBL:QIS11730.1,
RC ECO:0000313|Proteomes:UP000503540};
RX PubMed=31697466;
RA Herisse M., Ishida K., Porter J.L., Howden B., Hertweck C., Stinear T.P.,
RA Pidot S.J.;
RT "Identification and Mobilization of a Cryptic Antibiotic Biosynthesis Gene
RT Locus from a Human-Pathogenic Nocardia Isolate.";
RL ACS Chem. Biol. 0:0-0(2019).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP046172; QIS11730.1; -; Genomic_DNA.
DR RefSeq; WP_167474499.1; NZ_CP046172.1.
DR AlphaFoldDB; A0A6G9YF23; -.
DR KEGG; nah:F5544_19310; -.
DR Proteomes; UP000503540; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:SF23; D-ALANINE--D-ALANINE LIGASE B; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000503540}.
FT DOMAIN 127..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 325 AA; 34247 MW; 0467F7394B8992BC CRC64;
MLGGGESNER DVSAASAAAV IEALRASGHN VTAIDPATWP APARFSAQVG RNAPSEAEGA
RLAAAFRANL RDEAFWRAVD GEVIFLALHG GMGESGELKA ELESRGLVGT GASAAVMARS
WDKQDTVAEL AAAQVRVPRR LRPETDENGE LSWPEPTAGC IVKPALDGSS INVFKCATAD
EIAVAVKEID GPVLVEELLP GPEFTVGVVG SRVLPPVLIE PGEGWFGYEQ KYQAGRSREI
CPAPIDDVLR DELVELARRS VDVLGFGAES YARVDIMLDA AGRPCVLEVN SLPGLTGTSL
LPLAARAAGW DFPRLCAEIV RLATA
//
