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Database: UniProt
Entry: Q03AZ2
LinkDB: Q03AZ2
Original site: Q03AZ2 
ID   DLTA_LACC3              Reviewed;         506 AA.
AC   Q03AZ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   14-MAY-2014, entry version 56.
DE   RecName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1;
DE            EC=6.1.1.13;
DE   AltName: Full=D-alanine-D-alanyl carrier protein ligase;
DE            Short=DCL;
DE   AltName: Full=D-alanine-activating enzyme;
DE            Short=DAE;
GN   Name=dltA; OrderedLocusNames=LSEI_0794;
OS   Lactobacillus casei (strain ATCC 334).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of D-alanyl-lipoteichoic
CC       acid (LTA). Catalyzes an ATP-dependent two-step reaction where it
CC       forms a high energy D-alanyl AMP intermediate and transfers the
CC       alanyl residues from AMP to Dcp (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + D-alanine + poly(ribitol phosphate) =
CC       AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. DltA subfamily.
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DR   EMBL; CP000423; ABJ69630.1; -; Genomic_DNA.
DR   RefSeq; YP_806072.1; NC_008526.1.
DR   ProteinModelPortal; Q03AZ2; -.
DR   STRING; 321967.LSEI_0794; -.
DR   EnsemblBacteria; ABJ69630; ABJ69630; LSEI_0794.
DR   GeneID; 4419382; -.
DR   KEGG; lca:LSEI_0794; -.
DR   PATRIC; 22205274; VBILacCas62221_0795.
DR   eggNOG; COG1020; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; IANQAPF; -.
DR   OrthoDB; EOG6QP0WP; -.
DR   BioCyc; LCAS321967:GH4S-793-MONOMER; -.
DR   UniPathway; UPA00556; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047473; F:D-alanine-poly(phosphoribitol) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00593; DltA; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR010072; D_ala_DACP_lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR01734; D-ala-DACP-lig; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    506       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_1000025530.
SQ   SEQUENCE   506 AA;  56144 MW;  2138A161D2091C71 CRC64;
     MIDNVITAID RVAAEHPTRV AYDYEGTQYT YAQLKEGSDR LAGFFAETLP EHEPIIVYGG
     QTFDMVEVFL GLSKSGHAYI PIDTHSPNER ITQVQDVAHT PAIIEVAPLP IAVPDVQIIR
     APALHEAEKT HAPISSLQHA VVGDDNYYII FTSGTTGKPK GVQISHDNLL SYVNWNISDF
     GLKEGVVAMS QPPYSFDLSV MDLYPTLVLG GTLKALPKEV TDNFKTLFAT LPKLGLNEWV
     STPSFAEIAL LDPNFNQDNY PDLTHFLFCG EELVNKTAQE LITRFPKATV YNTYGPTETT
     VAVTGMAITQ DIVDQYPRLP IGFAKPDTEI FVVDEQGNQV SAGTEGELMI VGPSVSKGYL
     NNPEKTAKAF FNVGSQRGYR SGDLATMTED GMIFYRGRTD FQVKLHGYRI ELEDVDHNLN
     QVSYIKQAST VPRYNKDHKV AQLIAFAVAK PNDFESDMKL TQAVKAELGK MVMEYMIPQR
     IIYRDKLPLT ANGKVDRKAL IAEVNH
//
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