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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   28-FEB-2018, entry version 76.
DE   RecName: Full=D-alanine--D-alanyl carrier protein ligase {ECO:0000255|HAMAP-Rule:MF_00593};
DE            Short=DCL {ECO:0000255|HAMAP-Rule:MF_00593};
DE            EC=6.2.1.- {ECO:0000255|HAMAP-Rule:MF_00593};
DE   AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00593};
DE   AltName: Full=D-alanine-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00593};
DE            Short=DAE {ECO:0000255|HAMAP-Rule:MF_00593};
GN   Name=dltA {ECO:0000255|HAMAP-Rule:MF_00593};
GN   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: Catalyzes the first step in the D-alanylation of
CC       lipoteichoic acid (LTA), the activation of D-alanine and its
CC       transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-
CC       dependent two-step reaction, forms a high energy D-alanyl-AMP
CC       intermediate, followed by transfer of the D-alanyl residue as a
CC       thiol ester to the phosphopantheinyl prosthetic group of the Dcp.
CC       D-alanylation of LTA plays an important role in modulating the
CC       properties of the cell wall in Gram-positive bacteria, influencing
CC       the net charge of the cell wall. {ECO:0000255|HAMAP-
CC       Rule:MF_00593}.
CC   -!- CATALYTIC ACTIVITY: D-alanine + ATP + holo-[D-alanyl-carrier
CC       protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier
CC       protein]. {ECO:0000255|HAMAP-Rule:MF_00593}.
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00593}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00593}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. DltA subfamily. {ECO:0000255|HAMAP-Rule:MF_00593}.
DR   EMBL; CP000262; ABF38116.1; -; Genomic_DNA.
DR   RefSeq; WP_011528711.1; NC_008024.1.
DR   ProteinModelPortal; Q1J667; -.
DR   SMR; Q1J667; -.
DR   EnsemblBacteria; ABF38116; ABF38116; MGAS10750_Spy1166.
DR   KEGG; spi:MGAS10750_Spy1166; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NFYIIFT; -.
DR   OrthoDB; POG091H07SP; -.
DR   BioCyc; SPYO370554:G1G63-1167-MONOMER; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000002434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047473; F:D-alanine [D-alanyl carrier protein] ligase activity; IEA:InterPro.
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; DltA.
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--D-alanyl carrier protein
FT                                ligase.
FT                                /FTId=PRO_1000025539.
FT   NP_BIND     152    153       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     294    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     397    400       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     199    199       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
FT   BINDING     303    303       D-alanine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     385    385       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     499    499       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     499    499       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
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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