ID   I4B5R2_TURPD            Unreviewed;       334 AA.
AC   I4B5R2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:AFM12619.1};
GN   OrderedLocusNames=Turpa_1972 {ECO:0000313|EMBL:AFM12619.1};
OS   Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS   (Leptospira parva).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Turneriella.
OX   NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM12619.1, ECO:0000313|Proteomes:UP000006048};
RN   [1] {ECO:0000313|EMBL:AFM12619.1, ECO:0000313|Proteomes:UP000006048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC   {ECO:0000313|Proteomes:UP000006048};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL   Submitted (JUN-2012) 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; CP002959; AFM12619.1; -; Genomic_DNA.
DR   RefSeq; WP_014803126.1; NC_018020.1.
DR   AlphaFoldDB; I4B5R2; -.
DR   STRING; 869212.Turpa_1972; -.
DR   KEGG; tpx:Turpa_1972; -.
DR   PATRIC; fig|869212.3.peg.1976; -.
DR   HOGENOM; CLU_039268_2_0_12; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000006048; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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:AFM12619.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006048}.
FT   DOMAIN          115..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   334 AA;  38104 MW;  355220509FE7DD80 CRC64;
     MRVLVAFDFP TALPKNGDYR SLLHAEDWRP TRNVMEAIAR LGHEPILQGV YDDILPLVFT
     IKRKKPDIVF NLLESFRQKR HYEGALAGLF DLLQVPYTGC SAEALTICRN KSYTKLLLRH
     TKIKFPRSVV FPRGKTNRSI KDLKFPVIVK PLGLEGSDGI SQASFVADEA ACIERVKTLH
     ETYEVDALAE EYIEGREIYA GVLGLEKLTA LPLREMLFTN FPEDRPKFAT FHAKWNPEFR
     KKWGIKNTFA KGIDEKTQAD IEQISKSAFR ALGLSGFARL DLRLTDKNEI FVLEVNPNPN
     IANDDEIAYA SQRLGISYDQ LIQKLLDYGK RRRG
//