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Database: UniProt/TrEMBL
Entry: W8TRT0_STAAU
LinkDB: W8TRT0_STAAU
Original site: W8TRT0_STAAU 
ID   W8TRT0_STAAU            Unreviewed;       356 AA.
AC   W8TRT0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   20-JUN-2018, entry version 48.
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=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN   ECO:0000313|EMBL:KMR56067.1};
GN   ORFNames=BTN44_12750 {ECO:0000313|EMBL:AUS76040.1}, EP54_12800
GN   {ECO:0000313|EMBL:KMR56067.1}, EQ90_09645
GN   {ECO:0000313|EMBL:KMR36143.1}, RK60_10655
GN   {ECO:0000313|EMBL:AVG70035.1}, RK64_11055
GN   {ECO:0000313|EMBL:AVG64671.1}, RK68_01400
GN   {ECO:0000313|EMBL:AVG59989.1}, RK73_07925
GN   {ECO:0000313|EMBL:AVG58408.1}, RK98_09825
GN   {ECO:0000313|EMBL:AVG55858.1}, RL06_03450
GN   {ECO:0000313|EMBL:AVG49110.1}, SAMEA3448991_02378
GN   {ECO:0000313|EMBL:SGR80421.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:KMR56067.1};
RN   [1] {ECO:0000313|EMBL:KMR56067.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CA15 {ECO:0000313|EMBL:KMR36143.1}, and M121
RC   {ECO:0000313|EMBL:KMR56067.1};
RX   PubMed=26048971; DOI=10.1093/infdis/jiv320;
RA   Planet P.J., Diaz L., Kolokotronis S.O., Narechania A., Reyes J.,
RA   Xing G., Rincon S., Smith H., Panesso D., Ryan C., Smith D.P.,
RA   Guzman M., Zurita J., Sebra R., Deikus G., Nolan R.L., Tenover F.C.,
RA   Weinstock G.M., Robinson D.A., Arias C.A.;
RT   "Parallel Epidemics of Community-Associated Methicillin-Resistant
RT   Staphylococcus aureus USA300 Infection in North and South America.";
RL   J. Infect. Dis. 212:1874-1882(2015).
RN   [2] {ECO:0000313|EMBL:SGR80421.1, ECO:0000313|Proteomes:UP000243399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3688STDY6124981 {ECO:0000313|EMBL:SGR80421.1,
RC   ECO:0000313|Proteomes:UP000243399};
RG   Pathogen Informatics;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AUS76040.1, ECO:0000313|Proteomes:UP000236484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA107 {ECO:0000313|EMBL:AUS76040.1,
RC   ECO:0000313|Proteomes:UP000236484};
RA   Bian X., Wang M., Sun H., Fu J., Yu F., Dai L., Liu B., Shi J.;
RT   "Clinical isolated MRSA107 genomics characteristics of resistance to
RT   disinfectants.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000035281, ECO:0000313|Proteomes:UP000035309, ECO:0000313|Proteomes:UP000035452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_1 {ECO:0000313|EMBL:AVG70035.1}, FDAARGOS_10
RC   {ECO:0000313|EMBL:AVG59989.1}, FDAARGOS_15
RC   {ECO:0000313|EMBL:AVG58408.1}, FDAARGOS_40
RC   {ECO:0000313|EMBL:AVG55858.1}, FDAARGOS_48
RC   {ECO:0000313|EMBL:AVG49110.1}, FDAARGOS_6
RC   {ECO:0000313|EMBL:AVG64671.1}, HDE288
RC   {ECO:0000313|Proteomes:UP000035309,
RC   ECO:0000313|Proteomes:UP000035544}, NRS1
RC   {ECO:0000313|Proteomes:UP000035484}, NRS106
RC   {ECO:0000313|Proteomes:UP000035281}, NRS129
RC   {ECO:0000313|Proteomes:UP000035452}, and NRS152
RC   {ECO:0000313|Proteomes:UP000035463};
RA   Sichtig H., Tallon L., Sadzewicz L., Sengamalay N., Nagaraj S.,
RA   Vavikolanu K., Aluvathingal J., Nadendla S., Pirone D.C., Hoffman M.,
RA   Muruvanda T., Allard M., Evans P.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (FEB-2018) 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; CP018629; AUS76040.1; -; Genomic_DNA.
DR   EMBL; CP026953; AVG49110.1; -; Genomic_DNA.
DR   EMBL; CP026958; AVG55858.1; -; Genomic_DNA.
DR   EMBL; CP026960; AVG58408.1; -; Genomic_DNA.
DR   EMBL; CP026961; AVG59989.1; -; Genomic_DNA.
DR   EMBL; CP026962; AVG64671.1; -; Genomic_DNA.
DR   EMBL; CP026968; AVG70035.1; -; Genomic_DNA.
DR   EMBL; LALJ01000022; KMR36143.1; -; Genomic_DNA.
DR   EMBL; LALQ01000064; KMR56067.1; -; Genomic_DNA.
DR   EMBL; FQDK01000008; SGR80421.1; -; Genomic_DNA.
DR   RefSeq; WP_000159631.1; NZ_PQWV01000006.1.
DR   EnsemblBacteria; AOO99389; AOO99389; FORC27_2151.
DR   EnsemblBacteria; CFG07204; CFG07204; ERS093009_02280.
DR   EnsemblBacteria; CXE79052; CXE79052; ERS074020_01925.
DR   EnsemblBacteria; CXM26048; CXM26048; ERS072738_01964.
DR   EnsemblBacteria; CZQ30412; CZQ30412; ERS1058648_02019.
DR   EnsemblBacteria; OAP74134; OAP74134; A4U86_07315.
DR   EnsemblBacteria; SCR62068; SCR62068; SAMEA2298760_02275.
DR   KEGG; saud:CH52_08540; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000035281; Chromosome.
DR   Proteomes; UP000035309; Chromosome.
DR   Proteomes; UP000035452; Chromosome.
DR   Proteomes; UP000035463; Chromosome.
DR   Proteomes; UP000035484; Chromosome.
DR   Proteomes; UP000035544; Chromosome.
DR   Proteomes; UP000236484; Chromosome.
DR   Proteomes; UP000243399; 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_sf.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035281,
KW   ECO:0000313|Proteomes:UP000035309, ECO:0000313|Proteomes:UP000035452,
KW   ECO:0000313|Proteomes:UP000035463};
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:KMR56067.1};
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      134    339       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   COILED      148    168       {ECO:0000256|SAM:Coils}.
FT   METAL       293    293       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       306    306       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       306    306       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       308    308       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   356 AA;  40231 MW;  65822883958DC645 CRC64;
     MTKENICIVF GGKSAEHEVS ILTAQNVLNA IDKDKYHVDI IYITNDGDWR KQNNITAEIK
     STDELHLENG EALEISQLLK ESSSGQPYDA VFPLLHGPNG EDGTIQGLFE VLDVPYVGNG
     VLSAASSMDK LVMKQLFEHR GLPQLPYISF LRSEYEKYEH NILKLVNDKL NYPVFVKPAN
     LGSSVGISKC NNEAELKEGI KEAFQFDRKL VIEQGVNARE IEVAVLGNDY PEATWPGEVV
     KDVAFYDYKS KYKDGKVQLQ IPADLDEDVQ LTLRNMALEA FKATDCSGLV RADFFVTEDN
     QIYINETNAM PGFTAFSMYP KLWENMGLSY PELITKLIEL AKERHQDKQK NKYKID
//
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