Q03AZ0 (DLTC_LACC3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-alanine--poly(phosphoribitol) ligase subunit 2
EC=6.1.1.13

Alternative name(s):
D-alanyl carrier protein
Short name=DCP

Gene names

Name:	dltC
Ordered Locus Names:	LSEI_0796

Organism

Lactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP]

Taxonomic identifier

321967 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl substituent to membrane-associated LTA By similarity. HAMAP MF_00565
Catalytic activity	ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate). HAMAP MF_00565
Pathway	Cell wall biogenesis; lipoteichoic acid biosynthesis. HAMAP MF_00565
Post-translational modification	4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP By similarity. HAMAP MF_00565
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation
Ligand	ATP-binding Nucleotide-binding Phosphopantetheine
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW teichoic acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW D-alanine-poly(phosphoribitol) ligase activity Inferred from electronic annotation. Source: EC acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 81

81

D-alanine--poly(phosphoribitol) ligase subunit 2 HAMAP MF_00565

PRO_1000024914

Amino acid modifications

Modified residue

39

1

O-(pantetheine 4'-phosphoryl)serine Probable

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

81

Helix Strand Turn

Details...

Helix

4 – 7

4

Helix

11 – 17

7

Turn

21 – 25

5

Turn

31 – 33

3

Helix

43 – 49

7

Turn

64 – 66

3

Beta strand

67 – 69

3

Helix

70 – 78

9

Sequences

	Sequence		Length	Mass (Da)
	Q03AZ0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 24DBFC59AD86D47C	FASTA	81	8,865
	10 20 30 40 50 60 MADEAIKNGV LDILADLTGS DDVKTNLDLN LFETGLLDSM GTVQLLLELQ SQFGVEAPVS 70 80 EFDRSQWDTP NKIIAKVEQA Q

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 334.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000423 Genomic DNA. Translation: ABJ69632.1.

RefSeq

YP_806074.1. NC_008526.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HQB	NMR	-	A	2-81	[»]

ProteinModelPortal

Q03AZ0.

SMR

Q03AZ0. Positions 2-81.

ModBase

Search...

Protein-protein interaction databases

STRING

Q03AZ0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

4419384.

GenomeReviews

Gene locus LSEI_0796 in contig CP000423_GR.

KEGG

lca:LSEI_0796.

PATRIC

22205278. VBILacCas62221_0797.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0236.

HOGENOM

HBG516530.

OMA

QMDENIF.

ProtClustDB

PRK05087.

Enzyme and pathway databases

BioCyc

LCAS321967:LSEI_0796-MONOMER.

Family and domain databases

HAMAP

MF_00565. DltC.
[Tree]

InterPro

IPR009081. Acyl_carrier_prot-like.
IPR003230. D-ala_carrier.
IPR006163. Phsphopanteth-bd.
[Graphical view]

Gene3D

G3DSA:1.10.1200.10. ACP_like. 1 hit.

KO

K14188.

Pfam

PF00550. PP-binding. 1 hit.
[Graphical view]

SUPFAM

SSF47336. ACP_like. 1 hit.

TIGRFAMs

TIGR01688. DltC. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DLTC_LACC3

Accession

Primary (citable) accession number: Q03AZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program