ID A0A1E5G1A0_9FIRM Unreviewed; 714 AA.
AC A0A1E5G1A0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 27.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OEF96675.1};
GN ORFNames=BHF68_06245 {ECO:0000313|EMBL:OEF96675.1};
OS Desulfuribacillus alkaliarsenatis.
OC Bacteria; Bacillati; Bacillota; Desulfuribacillia; Desulfuribacillales;
OC Desulfuribacillaceae; Desulfuribacillus.
OX NCBI_TaxID=766136 {ECO:0000313|EMBL:OEF96675.1, ECO:0000313|Proteomes:UP000094296};
RN [1] {ECO:0000313|EMBL:OEF96675.1, ECO:0000313|Proteomes:UP000094296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AHT28 {ECO:0000313|EMBL:OEF96675.1,
RC ECO:0000313|Proteomes:UP000094296};
RA Abin C.A., Hollibaugh J.T.;
RT "Draft genome sequence for the type strain of Desulfuribacillus
RT alkaliarsenatis AHT28, an obligately anaerobic, sulfidogenic bacterium
RT isolated from Russian soda lake sediments.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEF96675.1}.
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DR EMBL; MIJE01000030; OEF96675.1; -; Genomic_DNA.
DR RefSeq; WP_069643258.1; NZ_MIJE01000030.1.
DR AlphaFoldDB; A0A1E5G1A0; -.
DR STRING; 766136.BHF68_06245; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000094296; Unassembled WGS sequence.
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 Gene3D; 3.30.70.360; -; 1.
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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OEF96675.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000094296}.
FT DOMAIN 119..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 80827 MW; 2BFA12758F94A976 CRC64;
MKIAIIYNRD SQAVINLFGK QNREKYGLQT INRIKNALKA QGHQVQAFEG DKNIIRKLEE
FMPSVISGER PGLVFNLSYG IQGRARYTHI PSILEMLGIP YVGSGPESHG IALDKVVTKM
ILIQKGLPTP KFAVLEKPDD PLDEALSYPM IVKPRDEAVS FGLKVVRNEQ ELREGVKFIY
DTFNGPTLVE EFIEGMEVNV GLLGNQPVEA LPPVELQFGE GEQIYTYEDK TKQSGRTVQH
VCPANLSPEQ SEQVQKLAID AFKAIGLFDS ARVDFRIDKE GNPYILEINS LASLGLGGSY
VYAANYVGLD YDKLVNRLVD VASQRYFGTP LASQLQTRTR DKRQAVFTYL TKNRDKIEEE
LKLWTNISSR TEDAVGLSTI VRKLDERLQK IGLHLSDELS NRRSVWTWET EEQKKEGTLL
VFPIDIPIER RVYPVPFRKD PEWLHGEGIA SSRAGIITVL YALSALKIIK KLKGKKIGVL
AYSDEGRGMR YSNTYLQMAA SNYEQVLVMN PGIYQGKVVD QRRGSRKYKV VIDGSSMRVG
SKVKKDVMSW FMERYDQISQ LNRPEDKLSV AVLDIHSDRY SILLSHRLQA NIYVNYLNSK
HADLVEKRLK EIFVVQDKEI HSNLEKLEER APLIRNRSTK KLIEQLKSIS EEWQLPFGVD
SSLLPSAAGV VPTKTPVLCG LAPASKDIYT PDEAIHRGEL LQRLLLLTLY LLKD
//
