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Database: UniProt/TrEMBL
Entry: R4QDL9_HELPX
LinkDB: R4QDL9_HELPX
Original site: R4QDL9_HELPX 
ID   R4QDL9_HELPX            Unreviewed;       347 AA.
AC   R4QDL9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=K751_04335 {ECO:0000313|EMBL:AGL71434.1};
OS   Helicobacter pylori UM066.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1321940 {ECO:0000313|EMBL:AGL71434.1, ECO:0000313|Proteomes:UP000013753};
RN   [1] {ECO:0000313|EMBL:AGL71434.1, ECO:0000313|Proteomes:UP000013753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UM066 {ECO:0000313|EMBL:AGL71434.1,
RC   ECO:0000313|Proteomes:UP000013753};
RA   Khosravi Y., Rehvathy V., Amoyo A., Seow S., Ong J., Susana W.,
RA   Primo B., Meredith A., Siddarth S., Pettersson S., Loke M., Goh K.,
RA   Vadivelu J.;
RT   "Draft Genome Sequences of Helicobacter pylori Strain UM037 and UM066
RT   using PacBio Sequencing Platform.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754451}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00754472};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00754454};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00644812}.
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DR   EMBL; CP005493; AGL71434.1; -; Genomic_DNA.
DR   RefSeq; WP_015642856.1; NZ_AUSJ01000004.1.
DR   EnsemblBacteria; AGL71434; AGL71434; K751_04335.
DR   KEGG; hpyu:K751_04335; -.
DR   PATRIC; fig|1321940.5.peg.879; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000013753; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 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 {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AGL71434.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00754442};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      134    332       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   347 AA;  39678 MW;  7019893E8169471C CRC64;
     MEFCVLFGGA SFEHEISIVS AIALKEALKD RIKYFIFLDE NHHFYLIEES NMHSKYFAQI
     KEKKLPPLIL TRNGLLKNSF LGAKIIELPL VINLVHGGDG EDGKLASLLE FYRIAFIGPR
     IEASVLSYNK YLTKLYAKDL GVKTLDYVLL NEKNRANALN LIGFNFPFIV KPSNAGSSLG
     VSVVKEEKEL IYALDGAFEY SKEVLIEPFI QGVKEYNLAG CKIKKNFCFS YIEEPNKQEF
     LDFKQKYLDF SRNKAPKANL SNALEEQLKE NFKKLYNDLF DGALIRCDFF VIENEVYLNE
     INPIPGSLAN YLFDDFKTTL ENLAQSLPKT PKIPIKNSYL LQIQKNK
//
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