ID DLTA_LISMF Reviewed; 510 AA.
AC Q721J2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 61.
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=LMOf2365_0994;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA Bayles D.O., Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT borne pathogen Listeria monocytogenes reveal new insights into the
RT core genome components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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; AE017262; AAT03772.1; -; Genomic_DNA.
DR RefSeq; YP_013595.1; NC_002973.6.
DR ProteinModelPortal; Q721J2; -.
DR STRING; 265669.LMOf2365_0994; -.
DR EnsemblBacteria; AAT03772; AAT03772; LMOf2365_0994.
DR GeneID; 2799331; -.
DR KEGG; lmf:LMOf2365_0994; -.
DR PATRIC; 20323214; VBILisMon105049_0997.
DR eggNOG; COG1020; -.
DR HOGENOM; HOG000229995; -.
DR KO; K03367; -.
DR OMA; DALACYL; -.
DR ProtClustDB; PRK04813; -.
DR UniPathway; UPA00556; -.
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 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1 510 D-alanine--poly(phosphoribitol) ligase
FT subunit 1.
FT /FTId=PRO_0000213147.
SQ SEQUENCE 510 AA; 57613 MW; 8AE9326D9D3A8FE5 CRC64;
MTTSIIERID AWAEKTPDFP CYEYAGTRLS YKELKRQSDA FGSFLLKNLN TDKEKPIIVY
GHMSPLMLVA FLGSIKSGRA YVPVDVSMPV ERIEQIKKAA DPSLFICTEE LPSNLTITGC
PVLTQDQLMD ALEKHFGEVP DKEACVKNDD NYYIIYTSGS TGNPKGVQIS QNNLVSFSNW
ILQDFSLSQG LRFLNQAPFS FDLSVMDLYP SLLSGGTLVP LDKTITANMK DLYREIPAQN
LDVWVSTPSF ADLCLLDDNF NQENNPGLIR FLFCGEVLAK KTASELLNRF PDAVIYNTYG
PTEATVAVTQ VKVTREVIDA YPSLPLGVIK PDMRLHIVDQ ETGEVLPEGE KGEIVLIGAS
VSKGYLNEPE KTDQVFFDYK GYQAYRTGDS GIIKDGYLFF QGRLDFQIKL HGYRIELEDI
ENNLKKVSYI QNCAIIPKMK DEKVDMLVAQ VIPTNHDFEK EYQLSAAIKN ELKEFMPAYM
IPRKWIYKTE FPLTMNGKID RKALNSEVNK
//
