ID H5YA84_9BRAD Unreviewed; 344 AA.
AC H5YA84;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ATP-grasp enzyme, D-alanine-D-alanine ligase {ECO:0000313|EMBL:EHR05839.1};
GN ORFNames=Bra471DRAFT_06671 {ECO:0000313|EMBL:EHR05839.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR05839.1};
RN [1] {ECO:0000313|EMBL:EHR05839.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR05839.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-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; CM001442; EHR05839.1; -; Genomic_DNA.
DR RefSeq; WP_007614841.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YA84; -.
DR HOGENOM; CLU_039268_2_0_5; -.
DR Proteomes; UP000005774; 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:EHR05839.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 118..331
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 344 AA; 38310 MW; 883B2A58A28C417D CRC64;
MRRLRILVLM HPDFVPPDSS DGHTAQEINA WKTEYDVVST LRAAGHEVRP LGAQEEIKPV
REAIEEFKPH VVFTLLEEFH NNVAFDQHIA SYLELMKVPY TGCNPRGLTL ARGKDLSKTL
VHHRRIAAPA FAVFPMRRKV KRPTRLALPL IVKSLNMDGS FGISQASIVD TDEKLAERVA
FIHERVESAA IAEQFIEGRE LYVGVLGNNR LRVLPVWELK FGSMGGRSSR HIATEKAKHD
TDYQEKVGIV DGPAKDLAPE VTARIQRAAK RIYRVLGLDG YARIDFRLTA DGTPYFIEAN
PNPEIAKSQE FATAALHAGL KYPALLQRIL ALGISRAKAG VSLG
//
