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 01-MAY-2013, entry version 52.
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; FCQEKMP; -.
DR ProtClustDB; PRK04813; -.
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 Pfam; PF00501; AMP-binding; 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
//
