ID F2CA65_STRSA Unreviewed; 516 AA.
AC F2CA65;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=D-alanine--D-alanyl carrier protein ligase {ECO:0000256|HAMAP-Rule:MF_00593};
DE Short=DCL {ECO:0000256|HAMAP-Rule:MF_00593};
DE EC=6.2.1.54 {ECO:0000256|HAMAP-Rule:MF_00593};
DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00593};
DE AltName: Full=D-alanine-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00593};
DE Short=DAE {ECO:0000256|HAMAP-Rule:MF_00593};
GN Name=dltA {ECO:0000256|HAMAP-Rule:MF_00593,
GN ECO:0000313|EMBL:EGF13171.1};
GN ORFNames=HMPREF9386_2057 {ECO:0000313|EMBL:EGF13171.1};
OS Streptococcus sanguinis SK330.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888813 {ECO:0000313|EMBL:EGF13171.1, ECO:0000313|Proteomes:UP000005955};
RN [1] {ECO:0000313|EMBL:EGF13171.1, ECO:0000313|Proteomes:UP000005955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK330 {ECO:0000313|EMBL:EGF13171.1,
RC ECO:0000313|Proteomes:UP000005955};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the D-alanylation of lipoteichoic
CC acid (LTA), the activation of D-alanine and its transfer onto the D-
CC alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step
CC reaction, forms a high energy D-alanyl-AMP intermediate, followed by
CC transfer of the D-alanyl residue as a thiol ester to the
CC phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA
CC plays an important role in modulating the properties of the cell wall
CC in Gram-positive bacteria, influencing the net charge of the cell wall.
CC {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanine + holo-[D-alanyl-carrier protein] = AMP + D-
CC alanyl-[D-alanyl-carrier protein] + diphosphate;
CC Xref=Rhea:RHEA:55132, Rhea:RHEA-COMP:14102, Rhea:RHEA-COMP:14103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:138620, ChEBI:CHEBI:456215;
CC EC=6.2.1.54; Evidence={ECO:0000256|HAMAP-Rule:MF_00593};
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC DltA subfamily. {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGF13171.1}.
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DR EMBL; AFBD01000009; EGF13171.1; -; Genomic_DNA.
DR RefSeq; WP_004189411.1; NZ_GL878550.1.
DR AlphaFoldDB; F2CA65; -.
DR PATRIC; fig|888813.3.peg.2026; -.
DR HOGENOM; CLU_000022_2_12_9; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000005955; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05945; DltA; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR HAMAP; MF_00593; DltA; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010072; DltA.
DR InterPro; IPR044507; DltA-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01734; D-ala-DACP-lig; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00593};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00593};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00593, ECO:0000313|EMBL:EGF13171.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00593}.
FT DOMAIN 14..366
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 424..503
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 156..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 203
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 298..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 307
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 401..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 503
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
SQ SEQUENCE 516 AA; 57278 MW; 8317C3B6C9EAC885 CRC64;
MSNKVIQDMI EAIEHFAQVQ PDFPVYDILG QVHTYGDLKK DSDSLAAQID RLGLPDKSPV
VVFGGQEYEM LATFVALTKS GHAYIPIDSH SALERVAAIV EVAEPSLIIA ISDFPLADVA
APIFSAEQVQ AAFREGASYE LSHPVQGDDN YYIIFTSGTT GKPKGVQISH NNLLSFTNWM
ITDKEFATPE RPQMLAQPPY SFDLSVMYWA PTLALGGTLF ALPSAVTQDF KQLFETILSL
PIAIWTSTPS FADMALLSDD FNSQKLPQLT HFYFDGEELT VKTAQKLRDR FPQARIINAY
GPTEATVALS AVAVTDEMLQ NCKRLPIGYT KADSPTFVID EEGQKVPNGQ QGEIIVCGPA
VSKGYLNNPE KTAEAFFEFE GLPAYHTGDV GSMTDEGLLL YGGRMDFQIK FNGFRIELED
VSQNLNKSKY VESAVAVPRY NKDHKVQNLL AYVILKDGVA EQFEREIDIT KAIKEDLQDI
MMSYMMPSKF LYRETLPLTP NGKIDIKGLI SEVNKR
//
