ID C7XXV4_9LACO Unreviewed; 509 AA.
AC C7XXV4;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:EEU29582.1};
GN ORFNames=HMPREF0501_01589 {ECO:0000313|EMBL:EEU29582.1};
OS Limosilactobacillus coleohominis 101-4-CHN.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=575594 {ECO:0000313|EMBL:EEU29582.1, ECO:0000313|Proteomes:UP000003987};
RN [1] {ECO:0000313|EMBL:EEU29582.1, ECO:0000313|Proteomes:UP000003987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101-4-CHN {ECO:0000313|EMBL:EEU29582.1,
RC ECO:0000313|Proteomes:UP000003987};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Liu Y., Xu Q., Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Lactobacillus coleohominis strain 101-4-CHN.";
RL Submitted (JUN-2009) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00593}.
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DR EMBL; GG698807; EEU29582.1; -; Genomic_DNA.
DR AlphaFoldDB; C7XXV4; -.
DR STRING; 575594.HMPREF0501_01589; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_12_9; -.
DR OrthoDB; 9765680at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000003987; 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; 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; 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:EEU29582.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00593};
KW Reference proteome {ECO:0000313|Proteomes:UP000003987}.
FT DOMAIN 11..363
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 422..497
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 154..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 200
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 295..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 304
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 497
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
SQ SEQUENCE 509 AA; 56726 MW; 6C3B0C020514CC66 CRC64;
MVTNIVPEID QIAKQHLDKV YFDEMGTTHT YQDLVNASNA LAAWLDYSNI PAGSPIMFYG
DHQFEMVAGF LGGLKSGHAY IPVETGSALP RMQSIINTAD PKLVIAVDDF PDQDLDYDGQ
ILNRFELRKI MDEQVSYNMD HEVAGDDTFY ILFTSGTTGS PKGIEISANN ITTFANWMLG
DDFDLPREAT FLGQPPFSFD ISHFYWLVGM LSGASVKAIP VKVVQNFGQL FKVLPDLKIN
VFFGTPSFAE LLLLSPDFNA EKMPDLQKFV FCGEELSVST VKRLFQKFPD AHIYNTYGPT
EATVAVTSCE ITRDMLKDAK RLPIGYDKPG VTTTIWDGDQ QITEPGKHGE IIISGDSVAA
GYLNNPEKTA KNFFKFNGQQ SYRTGDAGYI SADGLRHIIG RMDFQIKLHG FRVELDEVRS
SLELSQYIKQ AVAVPKYDKN GKATHLIAYV IAEPNDFASD TELTKAIRES LKDKIMDYMM
PTQFIYVDSY PTSANGKIAV KQLIAEANK
//
