ID A0A136KTH9_9CHLR Unreviewed; 354 AA.
AC A0A136KTH9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative D-alanine--D-alanine ligase {ECO:0000313|EMBL:KXK12701.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:KXK12701.1};
GN ORFNames=UZ14_CFX002002146 {ECO:0000313|EMBL:KXK12701.1};
OS Chloroflexi bacterium OLB14.
OC Bacteria; Chloroflexota; Tepidiformia.
OX NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK12701.1, ECO:0000313|Proteomes:UP000070321};
RN [1] {ECO:0000313|EMBL:KXK12701.1, ECO:0000313|Proteomes:UP000070321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB14 {ECO:0000313|EMBL:KXK12701.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK12701.1}.
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DR EMBL; LMZR01000049; KXK12701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KTH9; -.
DR STRING; 1617415.UZ14_CFX002002146; -.
DR PATRIC; fig|1617415.3.peg.2167; -.
DR Proteomes; UP000070321; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
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: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 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:KXK12701.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 118..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 354 AA; 39568 MW; 35CED16A55EFFADC CRC64;
MKSHWKIAVI ANIKNKYEPI PEGLPPDAFS DYDSIETIDA IRAALEVDGH TTTFIHADRT
LPYALQEYQP DFCFNIAEGL GGDAREAQVP ALLEILEIPY TASRVLANAI SLDKTLTKRI
WRDNGLPVSQ FQEFTTGNEE LEATFEFPLF VKPSREGTGM GIDAKAIVYS QKELNERIHY
LIKTYKQPAL VETFLSGREF TVGILGGSEA KVYSKNPTWY DEKGYHCFPI LELDTSHSNS
PWVYDNEAKS KDVGPPESPG YFCPAQIDSV LEAELKRLAI RAHETINALD VSRTDIRLDK
HGEPQLIEIN TLPGISPNYS DLCLQANAEG IAYADLVLDI LYLAAGRWGL IKEK
//
