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Database: UniProt
Entry: Q1J667
LinkDB: Q1J667
Original site: Q1J667 
ID   DLTA_STRPF              Reviewed;         512 AA.
AC   Q1J667;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   14-MAY-2014, entry version 58.
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=MGAS10750_Spy1166;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(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; CP000262; ABF38116.1; -; Genomic_DNA.
DR   RefSeq; YP_602660.1; NC_008024.1.
DR   ProteinModelPortal; Q1J667; -.
DR   STRING; 370554.MGAS10750_Spy1166; -.
DR   EnsemblBacteria; ABF38116; ABF38116; MGAS10750_Spy1166.
DR   GeneID; 4066705; -.
DR   KEGG; spi:MGAS10750_Spy1166; -.
DR   PATRIC; 19728603; VBIStrPyo25933_1196.
DR   eggNOG; COG1020; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NHDFEKE; -.
DR   OrthoDB; EOG6QP0WP; -.
DR   BioCyc; SPYO370554:GI3S-1221-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    512       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_1000025539.
SQ   SEQUENCE   512 AA;  56999 MW;  EE0161F667711B5F CRC64;
     MIKDMIDSIE QFAQTQADFP VYDCLGERRT YGQLKRDSDS IAAFIDSLAL LAKSPVLVFG
     AQTYDMLATF VALTKSGHAY IPVDVHSAPE RILAIIEIAK PSLIIAIEEF PLTIEGISLV
     SLSEIESAKL AEMPYERTHS VKGDDNYYII FTSGTTGQPK GVQISHDNLL SFTNWMIEDA
     AFDVPKQPQM LAQPPYSFDL SVMYWAPTLA LGGTLFALPK ELVADFKQLF TTIAQLPVGI
     WTSTPSFADM AMLSDDFCQA RMPALTHFYF DGEELTVSTA RKLFERFPSA KIINAYGPTE
     ATVALSAIEI TREMVDNYTR LPIGYPKPDS PTYIIDEDGK ELASGEQGEI IVTGPAVSKG
     YLNNPEKTAE AFFTFKGQPA YHTGDIGSLT EDNILLYGGR LDFQIKYAGY RIELEDVSQQ
     LNQSPMVASA VAVPRYNKEH KVQNLLAYIV VKDGVKERFD RELELTKAIK ASVKDHMMSY
     MMPSKFLYRD SLPLTPNGKI DIKTLINEVN NR
//
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