ID DLTA_STRZP Reviewed; 516 AA.
AC C1CNE9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
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=SPP_2228;
OS Streptococcus pneumoniae (strain P1031).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1031;
RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.;
RT "Complete genome sequence of Streptococcus pneumoniae strain P1031.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000920; ACO21603.1; -; Genomic_DNA.
DR RefSeq; YP_002739255.1; NC_012467.1.
DR ProteinModelPortal; C1CNE9; -.
DR STRING; 488223.SPP_2228; -.
DR EnsemblBacteria; ACO21603; ACO21603; SPP_2228.
DR GeneID; 7682790; -.
DR KEGG; spp:SPP_2228; -.
DR PATRIC; 32461838; VBIStrPne91701_2262.
DR eggNOG; COG1020; -.
DR HOGENOM; HOG000229995; -.
DR KO; K03367; -.
DR OMA; IAINDFP; -.
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 1 516 D-alanine--poly(phosphoribitol) ligase
FT subunit 1.
FT /FTId=PRO_1000146976.
SQ SEQUENCE 516 AA; 57427 MW; C20C9E7F8EB7150B CRC64;
MSNKPIADMI ETIEHFAQTQ PSYPVYNVLG QEHTYGDLKA DSDSLAAVID QLGLPEKSPV
VVFGGQEYEM LATFVALTKS GHAYIPIDSH SALERVSAIL EVAEPSLIIA ISAFPLEQVS
TPMINLAQVQ EAFAQGNNYE ITHPVKGDDN YYIIFTSGTT GKPKGVQISH DNLLSFTNWM
ITDKEFATPS RPQMLAQPPY SFDLSVMYWA PTLALGGTLF TLPSVITQDF KQLFAAIFSL
PIAIWTSTPS FADMAMLSEY FNSEKMPGIT HFYFDGEELT VKTAQKLRER FPNARIINAY
GPTEATVALS AVAVTDEMLA TLKRLPIGYT KADSPTFIID EEGNKLPNGE QGEIIVSGPA
VSKGYMNNPE KTAEAFFEFE DLPAYHTGDV GTMTDEGLLL YGGRMDFQIK FNGYRIELED
VSQNLNKSRF IESAVAVPRY NKDHKVQNLL AYVILKDGVR EQFERDIDIT KAIKEDLTDI
MMSYMMPSKF LYRDSLPLTP NGKIDIKGLI NEVNKR
//
