GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1Q2LGJ0_9HELI
LinkDB: A0A1Q2LGJ0_9HELI
Original site: A0A1Q2LGJ0_9HELI 
ID   A0A1Q2LGJ0_9HELI        Unreviewed;       349 AA.
AC   A0A1Q2LGJ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   ORFNames=XJ32_04495 {ECO:0000313|EMBL:AQQ59475.1};
OS   Helicobacter bilis.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=37372 {ECO:0000313|EMBL:AQQ59475.1, ECO:0000313|Proteomes:UP000188298};
RN   [1] {ECO:0000313|EMBL:AQQ59475.1, ECO:0000313|Proteomes:UP000188298}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAQJH {ECO:0000313|EMBL:AQQ59475.1,
RC   ECO:0000313|Proteomes:UP000188298};
RA   Conlan S., Thomas P.J., Mullikin J., Palmore T.N., Frank K.M.,
RA   Segre J.A.;
RT   "Whole genome sequencing of Helicobacter bilis strain AAQJH.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|SAAS:SAAS00644812}.
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; CP019645; AQQ59475.1; -; Genomic_DNA.
DR   KEGG; hbl:XJ32_04495; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000188298; 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-EC.
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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 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|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000188298};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AQQ59475.1};
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|SAAS:SAAS00644714}.
FT   DOMAIN      137    336       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   349 AA;  39447 MW;  85BDB150983D8C35 CRC64;
     MNLSIIFGGI SYEHEISIVS AITMAQKLGK NIKITHFIFL DSNHDFYLIE SSNMKSKYFS
     SLAYKQAKKI EIGVGGFYES GFLGKKKMLN TGLLLNLIHG GDGEDGVLSG LFDFYKIAYI
     GPRLEASILS YNKRLTKLYA KECGVETLPY YVLKRNETCE IPFELPYIIK PTCLGSSIGV
     CVVEDQTKLS YGLDCAFEFS NEVIMEPFKK GIKEYNLAGT KVNGEFILSL IEEPVKKDLL
     GFEDKYLDFS RTEEIKNAEI TESLTKNLHE AFKKIYNTTF EGALIRCDFF VSSDKIYLNE
     INPIPGSMAN YLFSDFESVL EKIATSLPRK HAININYQYI NQIQSAKGK
//
DBGET integrated database retrieval system