ID D5C222_NITHN Unreviewed; 350 AA.
AC D5C222;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:ADE16610.1};
GN OrderedLocusNames=Nhal_3587 {ECO:0000313|EMBL:ADE16610.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16610.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP001798; ADE16610.1; -; Genomic_DNA.
DR RefSeq; WP_013034459.1; NC_013960.1.
DR AlphaFoldDB; D5C222; -.
DR STRING; 472759.Nhal_3587; -.
DR KEGG; nhl:Nhal_3587; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_6; -.
DR OrthoDB; 9800957at2; -.
DR Proteomes; UP000001844; 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:ADE16610.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT DOMAIN 129..343
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 350 AA; 39457 MW; F8307D9FAC78CC7C CRC64;
MPAVRDDFCP PRELIFPHIT VILGDPRLPD ESKIGGRFSA EDIEAVDRVK EALGELQDYR
FTYLDNHSTL IANLTADPPD FVLNFCDTGY KNQARQELHI PALLEMLGIP YSGAGPTCLG
MCYDKSLVRS VARTHGIPVP AETFVRGNDR HGAVSQNFPV LIKPNRADGS LGITKDSLVH
DEQQARAYLN KLAMEFPNWD LLIQEFLPGE EYSVGVLGNP ASGFMILPIL AVDYSKLVAS
RLPPILAYAS KIDPQSPYWT DIKYCEASLK EDLRQRLVDY CLFLFERLGC RDYARFDFRT
DAQGEIKLLE VNPNPAWCWD GKLNLMAGFA GYHYAELLER ILHAAQVRYR
//
