GenomeNet

Database: UniProt/TrEMBL
Entry: F8E9J5_FLESM
LinkDB: F8E9J5_FLESM
Original site: F8E9J5_FLESM 
ID   F8E9J5_FLESM            Unreviewed;       301 AA.
AC   F8E9J5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   22-NOV-2017, entry version 47.
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   OrderedLocusNames=Flexsi_1677 {ECO:0000313|EMBL:AEI15324.1};
OS   Flexistipes sinusarabici (strain DSM 4947 / MAS 10).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Flexistipes.
OX   NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI15324.1, ECO:0000313|Proteomes:UP000006621};
RN   [1] {ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR039102-3};
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       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:SAAS00910642}.
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; CP002858; AEI15324.1; -; Genomic_DNA.
DR   RefSeq; WP_013886800.1; NC_015672.1.
DR   STRING; 717231.Flexsi_1677; -.
DR   EnsemblBacteria; AEI15324; AEI15324; Flexsi_1677.
DR   KEGG; fsi:Flexsi_1677; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; POG091H00GT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006621; 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   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; 2.
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:UP000006621};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AEI15324.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006621}.
FT   DOMAIN      105    294       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       249    249       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       261    261       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       261    261       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       263    263       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   301 AA;  32959 MW;  A437729F222CF79E CRC64;
     MINKNMRIVV LYGGFSSERE VSLTTGTAMG NSLKKNGYKN IIFMDIGGNF FKELLEIKPD
     ICVNGLHGKF GEDGKIQAVL ESLKIPYTGS GVAASCLAFD KAYSKYILRG AGLPTAEFVI
     ASKDNQKPPF LPCVVKPARE GSTIGISIVK QEAEYKRALK IAGQYDGKIV VEKFLDGKEI
     TVGILGDKAL PPIWIKPESG FYDYESKYTK GKTEYLFDTG CTEKEMAEIK DTALKAFNAA
     GCTGYGRVDF IYKENTPYIL EINTLPGMTE TSLLPQAAAE AGINFEQLVE EILYTSGESH
     D
//
DBGET integrated database retrieval system