ID A0A3Q9BJU7_9LACT Unreviewed; 410 AA.
AC A0A3Q9BJU7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:AZP04042.1};
GN ORFNames=EJN90_04790 {ECO:0000313|EMBL:AZP04042.1};
OS Jeotgalibaca ciconiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=2496265 {ECO:0000313|EMBL:AZP04042.1, ECO:0000313|Proteomes:UP000273326};
RN [1] {ECO:0000313|Proteomes:UP000273326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H21T32 {ECO:0000313|Proteomes:UP000273326};
RA Bae J.-W., Lee S.-Y.;
RT "Complete genome sequencing of Jeotgalibaca sp. H21T32.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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; CP034465; AZP04042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9BJU7; -.
DR KEGG; jeh:EJN90_04790; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000273326; Chromosome.
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: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 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 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 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 198..401
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 410 AA; 46104 MW; F32FD0A34C053E4E CRC64;
MPAVLLRTFT SFATTETTSS ARLKVKSDYK REILEKGIFD SSIIAIDLPH LTLRVTFSTS
VLSLGASITG CYNEKKDENT MEALAMHIVL VHSKYENVEE ARTTVDPMGA NRMATTVKAV
KDALEVSGHE VIPVEADYQL LSKIKKMKTP DLIFNLSTGI SDKRSQANVV GMLEMLHIPV
LGSRLTTHVL GLHKEITKSL LYAYNVRTAR YQLVEDENAP IRKDFIYPVI VKPEHEGSGI
GITASSKVDT PEKLRKIIME KIALHKQELL IEEYLPGREF TVGVMGNAHL EILPIKETVF
LDEDLKMLTY DLKMENDVMN KIPADIPEKL EDEIKSMVEK TYRILRCQDF ARIDIRLDAE
GKPTVMELNT YPGLVPDFSF FPMLAEAAGY SYAELINRLV EIALEPVVIQ
//