ID C5QLB0_9STAP Unreviewed; 361 AA. AC C5QLB0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 26-NOV-2014, entry version 30. 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 ECO:0000313|EMBL:EES42327.1}; GN ORFNames=HMPREF0793_0016 {ECO:0000313|EMBL:EES42327.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES42327.1}; RN [1] {ECO:0000313|EMBL:EES42327.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES42327.1}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047, CC ECO:0000256|SAAS:SAAS00083922}. CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D- CC alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047, CC ECO:0000256|SAAS:SAAS00084033}. CC -!- COFACTOR: CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00084031}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00083948}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047, CC ECO:0000256|SAAS:SAAS00083894}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP- CC Rule:MF_00047}. CC -!- SIMILARITY: Contains ATP-grasp domain. CC {ECO:0000256|SAAS:SAAS00084027}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES42327.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACJB01000001; EES42327.1; -; Genomic_DNA. DR ProteinModelPortal; C5QLB0; -. DR EnsemblBacteria; EES42327; EES42327; HMPREF0793_0016. DR PATRIC; 31399004; VBIStaEpi14170_2371. DR UniPathway; UPA00219; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. 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 PANTHER; PTHR23132; PTHR23132; 1. 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|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083940}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083934}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00084029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083911}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083964}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083963}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083938}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083966}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00083945}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047, KW ECO:0000256|SAAS:SAAS00084010}. FT DOMAIN 139 344 ATP-grasp. {ECO:0000256|HAMAP-Rule: FT MF_00047}. FT NP_BIND 172 227 ATP. {ECO:0000256|HAMAP-Rule:MF_00047}. FT METAL 298 298 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_00047}. FT METAL 311 311 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_00047}. FT METAL 311 311 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_00047}. FT METAL 313 313 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_00047}. SQ SEQUENCE 361 AA; 40819 MW; 803A5ACD717DA472 CRC64; MEENEMTKEN ICIVFGGKSA EHDVSILTAQ NVLNAINKDQ YQIDIIYITN EGEWKKKENI TEEIKNTDEL VLNDVEAGEI SQLLSKGSTG RSYDAVFPLL HGPNGEDGTI QGLFEVLDIP YVGNGVLAAS SSMDKLVMKQ LFEHRGLPQL PYISFLRSEY EKYENNIIKL VNDKLTYPVF VKPANLGSSV GISKCNNEKE LKSGIEEAFQ FDRKLVIEQG IEAREIEVAV LGNDYPETTW PGEVVKDVAF YDYKSKYKDG KVRLQIPAEL DQDVQMTLRN MALEAFKATD CSGLVRADFF VTEDNQIYIN ETNAMPGFTS FSMYPSLWEN MGLSYPDLIA KLIDLAKERH ADKKKNKYKI D //