ID A0A1F8MI53_9CHLR Unreviewed; 333 AA.
AC A0A1F8MI53;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OGN98286.1};
GN ORFNames=A2Y89_06010 {ECO:0000313|EMBL:OGN98286.1};
OS Chloroflexi bacterium RBG_13_51_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797624 {ECO:0000313|EMBL:OGN98286.1, ECO:0000313|Proteomes:UP000180314};
RN [1] {ECO:0000313|EMBL:OGN98286.1, ECO:0000313|Proteomes:UP000180314}
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:OGN98286.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGMR01000041; OGN98286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MI53; -.
DR Proteomes; UP000180314; 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:OGN98286.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 113..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 333 AA; 37216 MW; 764690C0E3927C62 CRC64;
MRIGLSYDLK TNATGHSAVD DAQEEYDSPE TVEIIAGALE KKRHRIIKLG GGTQFLDNIR
REEVDIVFNI SEGRGSYRSR EAQVPSVLEM LNIPYTGSDP LCLAICLDKA ITKKLVAAVN
IPTPRWLVIE EEPETQQIDW QGFPFPAIVK PAYEGSSKGI RLTSLAENIP QAEAEIARII
RNYHQPVMVE EFISGDEVTA GVIGNSPPRL VGMMRILPKK KEGHFVYSIE VKRDYLNLVE
YESPVQLPVP VLDKLEQYSL KAFKTLGCRD FSRVDFRIGR DGTPYFLEIN PLPGLGNYSD
LIIMAVKLGW THDEVIGAVL DAALERYPQC ISA
//
