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Database: UniProt
Entry: Q5XBN5
LinkDB: Q5XBN5
Original site: Q5XBN5 
ID   DLTA_STRP6              Reviewed;         512 AA.
AC   Q5XBN5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   20-DEC-2017, entry version 83.
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=M6_Spy1043;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus
RT   metagenome: complete genome sequence of a macrolide-resistant serotype
RT   M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87178.1; -; Genomic_DNA.
DR   RefSeq; WP_002989572.1; NC_006086.1.
DR   PDB; 3L8C; X-ray; 2.41 A; A/B=3-512.
DR   PDBsum; 3L8C; -.
DR   ProteinModelPortal; Q5XBN5; -.
DR   SMR; Q5XBN5; -.
DR   EnsemblBacteria; AAT87178; AAT87178; M6_Spy1043.
DR   KEGG; spa:M6_Spy1043; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NFYIIFT; -.
DR   UniPathway; UPA00556; -.
DR   EvolutionaryTrace; Q5XBN5; -.
DR   Proteomes; UP000001167; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    512       D-alanine--D-alanyl carrier protein
FT                                ligase.
FT                                /FTId=PRO_0000213167.
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}.
FT   HELIX         5     15       {ECO:0000244|PDB:3L8C}.
FT   STRAND       19     24       {ECO:0000244|PDB:3L8C}.
FT   STRAND       27     30       {ECO:0000244|PDB:3L8C}.
FT   HELIX        31     47       {ECO:0000244|PDB:3L8C}.
FT   STRAND       56     60       {ECO:0000244|PDB:3L8C}.
FT   HELIX        64     75       {ECO:0000244|PDB:3L8C}.
FT   STRAND       80     84       {ECO:0000244|PDB:3L8C}.
FT   HELIX        89     98       {ECO:0000244|PDB:3L8C}.
FT   STRAND      102    108       {ECO:0000244|PDB:3L8C}.
FT   STRAND      117    121       {ECO:0000244|PDB:3L8C}.
FT   HELIX       122    131       {ECO:0000244|PDB:3L8C}.
FT   STRAND      145    151       {ECO:0000244|PDB:3L8C}.
FT   STRAND      161    165       {ECO:0000244|PDB:3L8C}.
FT   HELIX       166    178       {ECO:0000244|PDB:3L8C}.
FT   TURN        180    182       {ECO:0000244|PDB:3L8C}.
FT   STRAND      189    191       {ECO:0000244|PDB:3L8C}.
FT   HELIX       199    201       {ECO:0000244|PDB:3L8C}.
FT   HELIX       202    210       {ECO:0000244|PDB:3L8C}.
FT   STRAND      214    217       {ECO:0000244|PDB:3L8C}.
FT   HELIX       220    222       {ECO:0000244|PDB:3L8C}.
FT   HELIX       226    235       {ECO:0000244|PDB:3L8C}.
FT   STRAND      239    243       {ECO:0000244|PDB:3L8C}.
FT   HELIX       245    252       {ECO:0000244|PDB:3L8C}.
FT   TURN        259    261       {ECO:0000244|PDB:3L8C}.
FT   STRAND      267    270       {ECO:0000244|PDB:3L8C}.
FT   HELIX       277    286       {ECO:0000244|PDB:3L8C}.
FT   STRAND      291    296       {ECO:0000244|PDB:3L8C}.
FT   HELIX       299    301       {ECO:0000244|PDB:3L8C}.
FT   STRAND      305    310       {ECO:0000244|PDB:3L8C}.
FT   HELIX       312    317       {ECO:0000244|PDB:3L8C}.
FT   STRAND      322    326       {ECO:0000244|PDB:3L8C}.
FT   STRAND      332    335       {ECO:0000244|PDB:3L8C}.
FT   STRAND      348    354       {ECO:0000244|PDB:3L8C}.
FT   HELIX       365    371       {ECO:0000244|PDB:3L8C}.
FT   STRAND      372    375       {ECO:0000244|PDB:3L8C}.
FT   STRAND      378    389       {ECO:0000244|PDB:3L8C}.
FT   STRAND      391    393       {ECO:0000244|PDB:3L8C}.
FT   STRAND      395    400       {ECO:0000244|PDB:3L8C}.
FT   HELIX       401    403       {ECO:0000244|PDB:3L8C}.
FT   HELIX       414    422       {ECO:0000244|PDB:3L8C}.
FT   STRAND      427    433       {ECO:0000244|PDB:3L8C}.
FT   STRAND      437    439       {ECO:0000244|PDB:3L8C}.
FT   STRAND      442    444       {ECO:0000244|PDB:3L8C}.
FT   STRAND      446    451       {ECO:0000244|PDB:3L8C}.
FT   HELIX       456    458       {ECO:0000244|PDB:3L8C}.
FT   HELIX       462    472       {ECO:0000244|PDB:3L8C}.
FT   HELIX       474    476       {ECO:0000244|PDB:3L8C}.
FT   HELIX       479    481       {ECO:0000244|PDB:3L8C}.
FT   STRAND      484    488       {ECO:0000244|PDB:3L8C}.
FT   STRAND      498    500       {ECO:0000244|PDB:3L8C}.
FT   HELIX       502    508       {ECO:0000244|PDB:3L8C}.
SQ   SEQUENCE   512 AA;  56987 MW;  330928DC894A6146 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 KMPALTHFYF DGEELTVSTA RKLFERFPSA KIINAYGPTE
     ATVALSAIEI TREMVDNYTR LPIGYPKPDS PTYIIDEDGK ELSSGEQGEI IVTGPAVSKG
     YLNNPEKTAE AFFTFKGQPA YHTGDIGSLT EDNILLYGGR LDFQIKYAGY RIELEDVSQQ
     LNQSPMVASA VAVPRYNKEH KVQNLLAYIV VKDGVKERFD RELELTKAIK ASVKDHMMSY
     MMPSKFLYRD SLPLTPNGKI DIKTLINEVN NR
//
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