ID   G2HVD0_9BACT            Unreviewed;       344 AA.
AC   G2HVD0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:BAK73083.1};
GN   ORFNames=ABLL_1208 {ECO:0000313|EMBL:BAK73083.1};
OS   Arcobacter sp. L.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Arcobacter.
OX   NCBI_TaxID=944547 {ECO:0000313|EMBL:BAK73083.1, ECO:0000313|Proteomes:UP000001290};
RN   [1] {ECO:0000313|EMBL:BAK73083.1, ECO:0000313|Proteomes:UP000001290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L {ECO:0000313|Proteomes:UP000001290};
RX   PubMed=22038970; DOI=10.1128/JB.06084-11;
RA   Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., Free A.,
RA   Taylor T.D.;
RT   "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter sp.
RT   Strain L, Both Isolated from a Microbial Fuel Cell.";
RL   J. Bacteriol. 193:6411-6412(2011).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; AP012048; BAK73083.1; -; Genomic_DNA.
DR   RefSeq; WP_014473919.1; NC_017192.1.
DR   AlphaFoldDB; G2HVD0; -.
DR   STRING; 944547.ABLL_1208; -.
DR   KEGG; arc:ABLL_1208; -.
DR   PATRIC; fig|944547.4.peg.1221; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_868573_0_0_7; -.
DR   Proteomes; UP000001290; 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   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   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   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000313|EMBL:BAK73083.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          127..333
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   344 AA;  40072 MW;  DC983C46704DB691 CRC64;
     MIIQNNTLSD QEVFIIKPFS KINKYIEIVT TPNSLRKTDM KDDLNVELIL EILSKNYEKV
     LVTTIKNEDD LKTLITKKPD LVFSRIKYFN FKKEKIWFSD YLKKHNIDYI SSNKNAFENE
     YDKNLAKQIV QKENINTANF FTTQPNEHEI ESLLPVTFPL FLKPEKKNNP EDINAQSVVF
     DFKKYQAKVL DIYNNQKSRT LVENYLSGKE YSVSILENKS KNILMILPVE IIACKNKNGH
     KILDFDARKS NLEEIIAITD KKIRKEVSSI AINSFRALGG KSIGKIDIKM SFNGIFHFLA
     ADFMPSLEEG YFYKAFFINE NMSYEEMILK IVDTNLSTPK EIEF
//