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Database: UniProt/TrEMBL
Entry: A0A0F0XTN6_9ENTR
LinkDB: A0A0F0XTN6_9ENTR
Original site: A0A0F0XTN6_9ENTR 
ID   A0A0F0XTN6_9ENTR        Unreviewed;       366 AA.
AC   A0A0F0XTN6; A0A0H0CPL9; A0A181CUC6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 22.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
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=ddlA {ECO:0000313|EMBL:SAZ05354.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=AN674_0210810 {ECO:0000313|EMBL:OEG92518.1},
GN   SAMEA3181516_00981 {ECO:0000313|EMBL:SAZ05354.1}, SS33_15630
GN   {ECO:0000313|EMBL:KJM88774.1};
OS   Enterobacter kobei.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=208224 {ECO:0000313|EMBL:KJM88774.1, ECO:0000313|Proteomes:UP000033742};
RN   [1] {ECO:0000313|EMBL:KJM88774.1, ECO:0000313|Proteomes:UP000033742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35730 {ECO:0000313|EMBL:KJM88774.1,
RC   ECO:0000313|Proteomes:UP000033742};
RA   McCorrison J., Sanka R., Adams M., Brinkac L., Nierman W., Sutton G.,
RA   Nelson K., Kiedrowski L., Guerrero D., Bonomo R.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SAZ05354.1, ECO:0000313|Proteomes:UP000078120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3380STDY6027363 {ECO:0000313|EMBL:SAZ05354.1,
RC   ECO:0000313|Proteomes:UP000078120};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OEG92518.1, ECO:0000313|Proteomes:UP000050321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST54:941713674 {ECO:0000313|EMBL:OEG92518.1,
RC   ECO:0000313|Proteomes:UP000050321};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910566}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
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}.
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DR   EMBL; JZYS01000027; KJM88774.1; -; Genomic_DNA.
DR   EMBL; LJED02000202; OEG92518.1; -; Genomic_DNA.
DR   EMBL; FKLS01000001; SAZ05354.1; -; Genomic_DNA.
DR   RefSeq; WP_014882727.1; NZ_LYUT01000050.1.
DR   EnsemblBacteria; KJM88774; KJM88774; SS33_15630.
DR   EnsemblBacteria; OEG92518; OEG92518; AN674_0210810.
DR   EnsemblBacteria; SAZ05354; SAZ05354; SAMEA3181516_00981.
DR   KEGG; ekb:BFV64_04660; -.
DR   PATRIC; fig|1619246.3.peg.2098; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000033742; Unassembled WGS sequence.
DR   Proteomes; UP000050321; Unassembled WGS sequence.
DR   Proteomes; UP000078120; 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: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   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 {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:UP000033742,
KW   ECO:0000313|Proteomes:UP000050321, ECO:0000313|Proteomes:UP000078120};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:KJM88774.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910590};
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      145    348       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       302    302       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       315    315       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       315    315       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       317    317       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   366 AA;  39233 MW;  E5282929E755603B CRC64;
     MAKQRVGIVF GGKSAEHEVS LQSAKNIVDA IDKSRFDVVL LGIDKQGQWH VNDASQYLLN
     AHDPAHIALN PSDISVATVP GVMKGQLIDA GNAQALTQID VVFPIVHGTL GEDGSLQGML
     RMANLPFVGS DVLGSAACMD KDVTKRLLRD AGLNIAPFVT LTRANRDKYS FAQVSGQLGL
     PLFVKPANQG SSVGVSKVAS EAEFTQAVRL AFEFDHKVVI EQGIKGREIE CAVLGNDFPQ
     ASTCGEVVLN SDFYSYDTKY IDDKGAQVVV PADIDPAIND KIRAIAISAY QTLGCSGMAR
     VDVFLTPEND VVINEINTLP GFTNISMYPK LWQASGLGYS ELITRLIELA LERHAADSAL
     KSSVNG
//
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