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Database: UniProt
Entry: Q5XBN5
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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   19-FEB-2014, entry version 67.
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=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 (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; 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   ProtClustDB; PRK04813; -.
DR   BioCyc; SPYO286636:GHNO-1103-MONOMER; -.
DR   UniPathway; UPA00556; -.
DR   EvolutionaryTrace; Q5XBN5; -.
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: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; D_ala_DACP_lig.
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
FT   STRAND       19     24
FT   STRAND       27     30
FT   HELIX        31     47
FT   STRAND       56     60
FT   HELIX        64     75
FT   STRAND       80     84
FT   HELIX        89     98
FT   STRAND      102    108
FT   STRAND      117    121
FT   HELIX       122    131
FT   STRAND      145    151
FT   STRAND      161    165
FT   HELIX       166    178
FT   TURN        180    182
FT   STRAND      189    191
FT   HELIX       199    201
FT   HELIX       202    210
FT   STRAND      214    217
FT   HELIX       220    222
FT   HELIX       226    235
FT   STRAND      239    243
FT   HELIX       245    252
FT   TURN        259    261
FT   STRAND      267    270
FT   HELIX       277    286
FT   STRAND      291    296
FT   HELIX       299    301
FT   STRAND      305    310
FT   HELIX       312    317
FT   STRAND      322    326
FT   STRAND      332    335
FT   STRAND      348    354
FT   HELIX       365    371
FT   STRAND      372    375
FT   STRAND      378    389
FT   STRAND      391    393
FT   STRAND      395    400
FT   HELIX       401    403
FT   HELIX       414    422
FT   STRAND      427    433
FT   STRAND      437    439
FT   STRAND      446    451
FT   HELIX       456    458
FT   HELIX       462    472
FT   HELIX       474    476
FT   HELIX       479    481
FT   STRAND      484    488
FT   STRAND      498    500
FT   HELIX       502    508
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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