ID F0SME8_RUBBR Unreviewed; 329 AA.
AC F0SME8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ADY62127.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:ADY62127.1};
GN OrderedLocusNames=Plabr_4556 {ECO:0000313|EMBL:ADY62127.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY62127.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP002546; ADY62127.1; -; Genomic_DNA.
DR RefSeq; WP_013630831.1; NC_015174.1.
DR AlphaFoldDB; F0SME8; -.
DR STRING; 756272.Plabr_4556; -.
DR KEGG; pbs:Plabr_4556; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_1_0; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000006860; Chromosome.
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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000313|EMBL:ADY62127.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000006860}.
FT DOMAIN 113..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 329 AA; 35958 MW; 38C8072A00A314E3 CRC64;
MLIGFTYDLR DDYLAEGYGE LETAEFDRVD TIDAIVDALV ACGHEVDRIG RAKQLVHRLA
DGCSWDLVFN ISEGLRGLSR ESQVPSILDV YEIPYTFSDP LTLSVCLHKE LTKQVVARAG
ILTPASLLVS QLSDLDRLHL QFPLFAKPVA EGTGKGVTPA SCVNSFNELH SVCLQLLTEF
EQPVLVESFL PGREFTVGIL GTGEAARVVG TLEIVLREAA EVGVYSYVNK ERCEDLVDYV
PVNGHDDAEV RQAEELALTA WRALGCRDGG RIDVRSDSHG RPNFIEANPL AGLHPHHSDL
PMIATAVGMT YVDLIDQIVT SAAERTVLA
//
