C5Q7L2 (C5Q7L2_STAEP) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP-Rule MF_00593
EC=6.1.1.13 HAMAP-Rule MF_00593

Alternative name(s):
D-alanine-D-alanyl carrier protein ligase HAMAP-Rule MF_00593
D-alanine-activating enzyme HAMAP-Rule MF_00593

Gene names

Name:	dltA HAMAP-Rule MF_00593 EMBL EES58844.1
ORF Names:	HMPREF0789_0586 EMBL EES58844.1

Organism

Staphylococcus epidermidis BCM-HMP0060 EMBL EES58844.1

Taxonomic identifier

525374 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus epidermidis

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp By similarity. HAMAP-Rule MF_00593 SAAS SAAS010071
Catalytic activity	ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate). HAMAP-Rule MF_00593 SAAS SAAS010071
Pathway	Cell wall biogenesis; lipoteichoic acid biosynthesis. HAMAP-Rule MF_00593 SAAS SAAS010071
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00593 SAAS SAAS010071.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily. HAMAP-Rule MF_00593

Ontologies

Keywords
Cellular component	Cytoplasm HAMAP-Rule MF_00593 SAAS SAAS010071
Ligand	ATP-binding HAMAP-Rule MF_00593 SAAS SAAS010071 Nucleotide-binding
Molecular function	Ligase HAMAP-Rule MF_00593 SAAS SAAS010072 EMBL EES58844.1
Gene Ontology (GO)
Biological_process	lipoteichoic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW D-alanine-poly(phosphoribitol) ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	C5Q7L2 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: B4B4025BD61F5892	FASTA	485	54,796
	10 20 30 40 50 60 MADLINILNH FVQEQPEAVA VRHTNDELTY KQLDEESSKL AHLLQDSKKP MILYGHMSPY 70 80 90 100 110 120 MIVGMIGAIK SGCGYVPIDT SVPKERVNMI IDKVQPEIIF NTSDETLEQT NAQVLKVSDI 130 140 150 160 170 180 QDSQYPIVFD SQMKQNDVVY TIFTSGSTGE PKGVQIEYAS LNEFAEWMVS LNKTGTGKEW 190 200 210 220 230 240 LNQAPFSFDL SVMAIYPCLT SGGTLNLVDK DMIKKPKLLN EMLVQTPMNV WVSTPSFIEM 250 260 270 280 290 300 CLLLPNLNEQ QYSSLKQFFF CGEILPHKTA KALVERFPNS MIYNTYGPTE ATVAVTSIQI 310 320 330 340 350 360 TEEILNQYNP LPVGVARPGT KLFATEEGEL VIEGQSVSLG YLKNEEKTTA VFNFEDGVRT 370 380 390 400 410 420 YHTGDKAKIE DGLWFIQGRI DFQIKLNGYR MELEEIETQL RQSKHVREAV VVPVYKNGKV 430 440 450 460 470 480 IHLIGAVVPT EPVEDNLAMT THIKHELKSR LPEYMIPRKF EWMEQLPLTS NGKLDRKKIA EVVNG

References

[1]

Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. , Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., Worley K., Gibbs R. Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BCM-HMP0060 EMBL EES58844.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACHE01000030 Genomic DNA. Translation: EES58844.1.
3D structure databases
ProteinModelPortal	C5Q7L2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EES58844; EES58844; HMPREF0789_0586.
PATRIC	31391518. VBIStaEpi34063_0861.
Enzyme and pathway databases
UniPathway	UPA00556.
Family and domain databases
HAMAP	MF_00593. DltA.
InterPro	IPR010071. AA_adenyl_domain. IPR000873. AMP-dep_Synth/Lig. IPR010072. D_ala_DACP_lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01733. AA-adenyl-dom. 1 hit. TIGR01734. D-ala-DACP-lig. 1 hit.
ProtoNet	Search...

Entry information

Entry name

C5Q7L2_STAEP

Accession

Primary (citable) accession number: C5Q7L2

Entry history

Integrated into UniProtKB/TrEMBL:	September 1, 2009
Last sequence update:	September 1, 2009
Last modified:	April 3, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)