ID Q89DI8_BRADU Unreviewed; 348 AA.
AC Q89DI8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Blr7451 protein {ECO:0000313|EMBL:BAC52716.1};
GN OrderedLocusNames=blr7451 {ECO:0000313|EMBL:BAC52716.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC52716.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; BA000040; BAC52716.1; -; Genomic_DNA.
DR RefSeq; NP_774091.1; NC_004463.1.
DR AlphaFoldDB; Q89DI8; -.
DR STRING; 224911.AAV28_34940; -.
DR EnsemblBacteria; BAC52716; BAC52716; BAC52716.
DR KEGG; bja:blr7451; -.
DR PATRIC; fig|224911.5.peg.7669; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_5; -.
DR InParanoid; Q89DI8; -.
DR OrthoDB; 9813261at2; -.
DR PhylomeDB; Q89DI8; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 122..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 348 AA; 38914 MW; 451865760D22CEAF CRC64;
MDRAMRRLRI LVLMHPDFMP PDSSDGYTAQ EINAWKTEYD VVSTLRAAGH EVRALGAQDE
IKPVREAIEE FKPHVVFTLL EEFHNNVAYD QHIASYLELM KVPYTGCNPR GLILARGKDL
SKTLVHHRRI AAPAFAVFPM RRKVKRPTRL ALPLIVKSLN MDGSFGISQA SIVDTDEKLA
ERVAFIHERV ESAAIAEQFI EGRELYVGVL GNNRLRVLPI WELKFGSMGG RRSRHIATEK
AKHDTDYQEK VGIVDGPAKD LAPEVTARIQ RAAKRIYRAL GLDGYARIDF RLAADGTPYF
IEANPNPEIA KSQEFATAAQ HAGLKYPDLL QRILALGISR AKAGVSLG
//
