ID DDL_BARHE Reviewed; 306 AA.
AC Q6G2Q8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 16-JAN-2019, entry version 89.
DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; OrderedLocusNames=BH11210;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic
RT derivative of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00047}.
DR EMBL; BX897699; CAF27906.1; -; Genomic_DNA.
DR RefSeq; WP_011180969.1; NZ_LRIJ02000001.1.
DR ProteinModelPortal; Q6G2Q8; -.
DR SMR; Q6G2Q8; -.
DR STRING; 283166.BH11210; -.
DR PaxDb; Q6G2Q8; -.
DR PRIDE; Q6G2Q8; -.
DR EnsemblBacteria; CAF27906; CAF27906; BH11210.
DR GeneID; 29621894; -.
DR KEGG; bhe:BH11210; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; YETKYTE; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_00047; Dala_Dala_lig; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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_sf.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 1.
DR SUPFAM; SSF52440; SSF52440; 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 1 306 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000030429.
FT DOMAIN 102 300 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 128 183 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 253 253 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 267 267 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 267 267 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 269 269 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 306 AA; 33259 MW; B5742195A9678D17 CRC64;
MKDEHIAVLM GGFSSERSVS LSSGTACADV LEAQGYRVSR VDVDGHIASV LEQLQPDIAF
NALHGPFGED GRIQGVLEYL KIPYTHSGVM ASALAMDKGR AKIVVASVGV SIAPSCVMSR
FAVGKEHPME PPYVIKPVCE GSSLGVIIVK ENESVPSLNV VGSEWVYADT VIVEKYIPGR
ELTCAVMGNK ALDVCEILPE KHFQFYDYDS KYKSGGSLHV CPAQLSSNIY QNVQRMSLAA
HQAIGCRGVS RSDFRFDEET GELVWLEINT QPGMTPTSLF PDIAKASGRT YGDIVQWMVE
DASCMR
//
