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 01-MAY-2013, entry version 50.
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; NDFDSEM; -.
DR ProtClustDB; CLSK2317801; -.
DR BioCyc; LCAS321967:GH4S-853-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: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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR010072; D_ala_DACP_lig.
DR InterPro; IPR025110; DUF4009.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; DUF4009; 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
//
