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Database: UniProt
Entry: A0A3Q9BJU7_9LACT
LinkDB: A0A3Q9BJU7_9LACT
Original site: A0A3Q9BJU7_9LACT 
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
//
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