ID A0A1F5B514_9BACT Unreviewed; 333 AA.
AC A0A1F5B514;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OGD25671.1};
GN ORFNames=A2V57_07125 {ECO:0000313|EMBL:OGD25671.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_65_30.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797277 {ECO:0000313|EMBL:OGD25671.1, ECO:0000313|Proteomes:UP000177619};
RN [1] {ECO:0000313|EMBL:OGD25671.1, ECO:0000313|Proteomes:UP000177619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD25671.1}.
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DR EMBL; MEYF01000126; OGD25671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5B514; -.
DR STRING; 1797277.A2V57_07125; -.
DR Proteomes; UP000177619; 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 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 InterPro; IPR016185; PreATP-grasp_dom_sf.
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 SUPFAM; SSF52440; PreATP-grasp domain; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGD25671.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 90..305
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 36780 MW; 932FEBFE4114EDF7 CRC64;
MLAECDSDET IAAVGQALRE RHQVVFIESD DKAYGRLKRQ RPHLVFNIAE RVVGPNRESH
IPTVCEMLDI PYTGSDPLTL GLCLVKSRAK EILSYHRIPN PAFWIVESAA AIPAGVRLPA
IVKPLFEGSS KGIKNNSLVH SLGELYERVE EVVAAYKQPV IVERFLAGRE FTVGVLGNTP
NCEILPIVEI DHGQLPAGAA PIYSYEAKWL WDTPARPLEI FKCPAPIPAV LRAKIGNVVA
RTCAVLRIRD WARIDVRLDD KGEPNILEVN PLPGILPNPE DNSCLPKAAR TAGYSYSDLI
HRVVEEASKR YGLRPTRTRP AASERPAVLA DRA
//
