ID A0A1F8RBH3_9CHLR Unreviewed; 333 AA.
AC A0A1F8RBH3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OGO44571.1};
GN ORFNames=A2137_05785 {ECO:0000313|EMBL:OGO44571.1};
OS Chloroflexi bacterium RBG_16_58_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797655 {ECO:0000313|EMBL:OGO44571.1, ECO:0000313|Proteomes:UP000180317};
RN [1] {ECO:0000313|EMBL:OGO44571.1, ECO:0000313|Proteomes:UP000180317}
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:OGO44571.1}.
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DR EMBL; MGNW01000015; OGO44571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RBH3; -.
DR Proteomes; UP000180317; 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:SF25; D-ALANINE--D-ALANINE LIGASE A; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGO44571.1};
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; 36924 MW; 475C62A371386CC1 CRC64;
MRIGLSYDLK TAITGRHTND DALEEYDSPE TVEIIAGALE SRGHTAVRLG GGVPLLDKLR
REKLDMVFNI AEGRGNYRSR EAQVPSLLEM LEIPYTGSDP ECLAVCLDKP LAKKLAAAEG
IRTPKWLVVA DQGEMDRAAW QGFPFPAIVK PAFEGSSKGI RLTSLVADAR QAQQEVRRIL
EGYRQPVMVE EFIDGDEVTV GIIGNRPPKL VGMMRIIPKK KVEHFVYSVE VKRDYVNLVD
YESPVRLPAK VLDMMESCSL KAFKTLGCRD FARVDFRIGG DGMPYFIEIN PLPGLGSYSD
LIIMATKMGW THHGVIGAVL EAAVERYPQC RAA
//