UniProt: A0A347VTN9

Database: UniProt
Entry: A0A347VTN9_9HELI

LinkDB:  A0A347VTN9_9HELI 
Original site:  A0A347VTN9_9HELI

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (3)   
Literature (2)   
   PubMed (2)   
All databases (25)   

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ID   A0A347VTN9_9HELI        Unreviewed;       349 AA.
AC   A0A347VTN9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
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=DCO61_06490 {ECO:0000313|EMBL:MWV69658.1}, LS64_001185
GN   {ECO:0000313|EMBL:TLD95511.1};
OS   Helicobacter saguini.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1548018 {ECO:0000313|EMBL:TLD95511.1, ECO:0000313|Proteomes:UP000029714};
RN   [1] {ECO:0000313|EMBL:TLD95511.1, ECO:0000313|Proteomes:UP000029714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95511.1,
RC   ECO:0000313|Proteomes:UP000029714};
RX   PubMed=25428971;
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Draft genome sequences of eight enterohepatic helicobacter species
RT   isolated from both laboratory and wild rodents.";
RL   Genome Announc. 2:e01218-e01214(2014).
RN   [2] {ECO:0000313|EMBL:TLD95511.1, ECO:0000313|Proteomes:UP000029714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95511.1,
RC   ECO:0000313|Proteomes:UP000029714};
RX   PubMed=27245408; DOI=.1128/IAI.00235-16;
RA   Shen Z., Mannion A., Whary M.T., Muthupalani S., Sheh A., Feng Y., Gong G.,
RA   Vandamme P., Holcombe H.R., Paster B.J., Fox J.G.;
RT   "Helicobacter saguini, a Novel Helicobacter Isolated from Cotton-Top
RT   Tamarins with Ulcerative Colitis, Has Proinflammatory Properties and
RT   Induces Typhlocolitis and Dysplasia in Gnotobiotic IL-10-/- Mice.";
RL   Infect. Immun. 84:2307-2316(2016).
RN   [3] {ECO:0000313|EMBL:TLD95511.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95511.1};
RA   Sheh A., Shen Z., Mannion A.J., Fox J.G.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MWV69658.1, ECO:0000313|Proteomes:UP000477070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-048 {ECO:0000313|EMBL:MWV69658.1}, and 16-048 (F4)
RC   {ECO:0000313|Proteomes:UP000477070};
RA   Mannion A., Shen Z., Fox J.G.;
RT   "Multi-Generational Helicobacter saguini Isolates.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00047};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TLD95511.1}.
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DR   EMBL; QBIU01000001; MWV69658.1; -; Genomic_DNA.
DR   EMBL; JRMP02000002; TLD95511.1; -; Genomic_DNA.
DR   RefSeq; WP_034573365.1; NZ_QBIX01000001.1.
DR   AlphaFoldDB; A0A347VTN9; -.
DR   STRING; 1548018.LS64_12140; -.
DR   OrthoDB; 9813261at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029714; Unassembled WGS sequence.
DR   Proteomes; UP000477070; Unassembled WGS sequence.
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:InterPro.
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; 3.40.50.20; -; 1.
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   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   NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00047};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000029714}.
FT   DOMAIN          137..332
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   349 AA;  39072 MW;  23722BEC299EAB29 CRC64;
     MKLSLLFGGA SFEHEISIVS AITILQKLKG KHEISACIFL DGEHNFYLIE SKNMTSKYFS
     SQDFKKAKRL EIGMGGFYES GMLGKKKLVV SNVILNLIHG GDGEDGVLAG LFSFFNIKFI
     GPRLEASTIS FNKHLTKLYA KEIGVNALPY AILKRGDTPN LPFDFPIIIK PTCLGSSIGV
     NIANDSKELE YALDSAFEYS DEVIIEPFIK GVREYNLAGA RLDSKFIFSV VEEPQKKDLL
     NFDDKYLDFS RTSEVLSAEI SESLKGEMQG IFKKIYGEMF CGALIRCDFF VIDSKIYLNE
     INPIPGSMAN YLFENFESVL ESLANALPRT NHIKINYNYI NKIQSAKGK
//

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