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 01-MAY-2013, entry version 62.
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; FCQEKMP; -.
DR ProtClustDB; PRK04813; -.
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: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 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
//
