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Entry: Q5XBN5
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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   26-NOV-2014, entry version 72.
DE   RecName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00593};
DE            EC=6.1.1.13 {ECO:0000255|HAMAP-Rule:MF_00593};
DE   AltName: Full=D-alanine-D-alanyl carrier protein ligase {ECO:0000255|HAMAP-Rule:MF_00593};
DE            Short=DCL {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: 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. {ECO:0000255|HAMAP-
CC       Rule:MF_00593}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-alanine + poly(ribitol phosphate) =
CC       AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).
CC       {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}.
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DR   EMBL; CP000003; AAT87178.1; -; Genomic_DNA.
DR   RefSeq; YP_060361.1; NC_006086.1.
DR   PDB; 3L8C; X-ray; 2.41 A; A/B=3-512.
DR   PDBsum; 3L8C; -.
DR   ProteinModelPortal; Q5XBN5; -.
DR   STRING; 286636.M6_Spy1043; -.
DR   EnsemblBacteria; AAT87178; AAT87178; M6_Spy1043.
DR   GeneID; 2941773; -.
DR   KEGG; spa:M6_Spy1043; -.
DR   PATRIC; 19724266; VBIStrPyo30273_1078.
DR   eggNOG; COG1020; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NHDFEKE; -.
DR   OrthoDB; EOG6QP0WP; -.
DR   BioCyc; SPYO286636:GHNO-1103-MONOMER; -.
DR   UniPathway; UPA00556; -.
DR   EvolutionaryTrace; Q5XBN5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047473; F:D-alanine-poly(phosphoribitol) ligase activity; IEA:UniProtKB-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; 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--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_0000213167.
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      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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