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Database: UniProt
Entry: A0A1F8RBH3_9CHLR
LinkDB: A0A1F8RBH3_9CHLR
Original site: A0A1F8RBH3_9CHLR 
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
//
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