GenomeNet

Database: UniProt
Entry: C1CNE9
LinkDB: C1CNE9
Original site: C1CNE9 
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   20-DEC-2017, entry version 56.
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=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;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae
RT   and closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO21603.1; -; Genomic_DNA.
DR   RefSeq; WP_000066732.1; NC_012467.1.
DR   ProteinModelPortal; C1CNE9; -.
DR   SMR; C1CNE9; -.
DR   EnsemblBacteria; ACO21603; ACO21603; SPP_2228.
DR   KEGG; spp:SPP_2228; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NFYIIFT; -.
DR   UniPathway; UPA00556; -.
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; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    516       D-alanine--D-alanyl carrier protein
FT                                ligase.
FT                                /FTId=PRO_1000146976.
FT   NP_BIND     156    157       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     298    303       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     401    404       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     203    203       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
FT   BINDING     307    307       D-alanine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     389    389       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     503    503       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     503    503       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
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
//
DBGET integrated database retrieval system