ID DDL_HERAR Reviewed; 334 AA.
AC A4G8T6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 51.
DE RecName: Full=D-alanine--D-alanine ligase;
DE EC=6.3.2.4;
DE AltName: Full=D-Ala-D-Ala ligase;
DE AltName: Full=D-alanylalanine synthetase;
GN Name=ddl; OrderedLocusNames=HEAR2809;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M.,
RA Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S.,
RA Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier P.,
RA Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D.,
RA van Dorsselaer A., Weiss S., Weissenbach J., Lett M.-C., Danchin A.,
RA Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-
RT rich environments.";
RL PLoS Genet. 3:518-530(2007).
CC -!- FUNCTION: Cell wall formation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC alanyl-D-alanine.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CU207211; CAL62923.1; -; Genomic_DNA.
DR RefSeq; YP_001101044.1; NC_009138.1.
DR ProteinModelPortal; A4G8T6; -.
DR STRING; 204773.HEAR2809; -.
DR PRIDE; A4G8T6; -.
DR EnsemblBacteria; CAL62923; CAL62923; HEAR2809.
DR GeneID; 4930494; -.
DR KEGG; har:HEAR2809; -.
DR PATRIC; 22115568; VBIHerArs17568_2642.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; WREAARY; -.
DR ProtClustDB; PRK01372; -.
DR BioCyc; HARS204773:GJCA-2702-MONOMER; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005618; C:cell wall; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_00047; Dala_Dala_lig; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR PANTHER; PTHR23132; PTHR23132; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 2.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT CHAIN 1 334 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000341110.
FT DOMAIN 111 315 ATP-grasp.
FT NP_BIND 141 196 ATP (By similarity).
FT METAL 268 268 Magnesium or manganese 1 (By similarity).
FT METAL 282 282 Magnesium or manganese 1 (By similarity).
FT METAL 282 282 Magnesium or manganese 2 (By similarity).
FT METAL 284 284 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 334 AA; 35913 MW; D433204BAAE28691 CRC64;
MTTTVQNLKA EFGKVGVLFG GRSAEREVSL MSGKGVLAAL QSKGVDAHAF DPAERSLAEL
AAEKFDRVFI ALHGSYGEDG TLQGALEQLG IPYTGPGVMA SAISMDKVMT KRVCLSHGVP
TPRFTVLDAE TTSAAQLQSV AAEFGLPLML KAPHEGSTIG IAKVETAEGM QAGFDLCAKY
EAVVLVEQFV KGRELTVPVI GSGRNARALP IVEIRAPQGN YDYEHKYFSN DTEYLCPAPF
DEAFTKRVQA LAVSAFNAVG CTGWSRVDFM VRASDNEPFL LEINTSPGMT SHSLVPMSAK
VAGTGYEDLC IEILRSAKTE LKPSSHMQLQ EQER
//
