ID D6YTD3_WADCW Unreviewed; 642 AA.
AC D6YTD3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN Name=ddlA1 {ECO:0000313|EMBL:ADI37394.1};
GN OrderedLocusNames=wcw_0017 {ECO:0000313|EMBL:ADI37394.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37394.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI37394.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(2010).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP001928; ADI37394.1; -; Genomic_DNA.
DR RefSeq; WP_013181122.1; NZ_LVEB01000016.1.
DR AlphaFoldDB; D6YTD3; -.
DR STRING; 716544.wcw_0017; -.
DR KEGG; wch:wcw_0017; -.
DR eggNOG; COG1181; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_430627_0_0_0; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000001505; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 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 Gene3D; 2.20.25.110; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_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 Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505}.
FT DOMAIN 402..614
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 642 AA; 73381 MW; 7F39B4FDDBB80B82 CRC64;
MNIKTAKCLG PVADLEKHLP VDWWRSIFNS IYLKTDADVV ENDTATAHEI DIFLNFSKIE
PSDHILDLCC GQGRHSLELA KRGYRFITGI DRSRYLIRLA RSRSQKLGYP IKFSEGDARK
IKLADQSMDC VMMMGNSFGY FEQERDDLKV LKEANRVLCE GGLLYLDVTN GAWMKENYEK
RSWEWISEEL MVCRERHLAT DLCRLISREL VTHAEKGVIA DQFYAERLYS FEELKSLLLA
AGFENIEQQD SLKGESFRNQ DLGMMANRIL ITAIAPKKRK PATRKNPFKI PCTVLLGDPR
IPDAIKRDGQ FNLEDFHTIN QMKEALKKIE NFQFSCFDDH KNLIRKFSQN PPPFVMNLCD
EGWNNDPFME LHPTALMEML KIPYTGAGPE CLSICYNKST VRAIAQSMDV HVPSEIWIDP
SNHSAAIPSI FPALIKPAYG DSSIGITQNA VVYSAEELVT YFDNLKAQMP NIPILIQEFL
DGREFSVGVI GNGVSLEVLP ILEVDYSGLP ENLPKILGYE SKWHPESPYC THIRYHQAHL
DESLARDLID TSINLFQRLK CRDYARFDFR MDSQGEAKLL EANPNPGWCW DGKMALMAEF
AGIQYHELLE KILKAAAERY PYLEHAETDS FSNKAAQKLK KS
//
