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Protein

Putative long chain fatty acid-CoA ligase VraA

Gene

vraA

Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciSAUR418127:GJP9-590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative long chain fatty acid-CoA ligase VraA (EC:6.2.1.-)
Alternative name(s):
Acyl-CoA synthetase
Gene namesi
Name:vraA
Ordered Locus Names:SAHV_0573
OrganismiStaphylococcus aureus (strain Mu3 / ATCC 700698)
Taxonomic identifieri418127 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Putative long chain fatty acid-CoA ligase VraAPRO_0000193190Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9KWK5.
SMRiQ9KWK5. Positions 8-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000279836.
OMAiWFESVCK.
OrthoDBiEOG64FKGZ.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KWK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVILEQLKT HTQNKPNDIA LHIDDETITY SQLNARITSA VESLQKYSLN
60 70 80 90 100
PVVAINMKSP VQSIICYLAL HRLHKVPMMM EGKWQSTIHR QLIEKYGIKD
110 120 130 140 150
VIGDTGLMQN IDSPMFIDST QLQHYPNLLH IGFTSGTTGL PKAYYRDEDS
160 170 180 190 200
WLASFEVNEM LMLKNENAIA APGPLSHSLT LYALLFALSS GRTFIGQTTF
210 220 230 240 250
HPEKLLNQCH KISSYKVAMF LVPTMIKSLL LVYNNEHTIQ SFFSSGDKLH
260 270 280 290 300
SSIFKKIKNQ ANDINLIEFF GTSETSFISY NLNQQAPVES VGVLFPNVEL
310 320 330 340 350
KTTNHDHNGI GTICIKSNMM FSGYVSEQCI NNDEWFVTND NGYVKEQYLY
360 370 380 390 400
LTGRQQDMLI IGGQNIYPAH VERLLTQSSS IDEAIIIGIP NERFGQIGVL
410 420 430 440 450
LYSGDVTLTH KNVKQFLKKK VKRYEIPSMI HHVEKMYYTA SGKIAREKMM

SMYLRGEL
Length:458
Mass (Da):52,024
Last modified:December 4, 2007 - v3
Checksum:i0843B823F1F5267B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591E → Q in BAB03327 (PubMed:10708580).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035449 Genomic DNA. Translation: BAB03327.2.
AP009324 Genomic DNA. Translation: BAF77456.1.
RefSeqiWP_001100835.1. NC_009782.1.

Genome annotation databases

EnsemblBacteriaiBAF77456; BAF77456; SAHV_0573.
KEGGisaw:SAHV_0573.
PATRICi19556115. VBIStaAur127830_0578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035449 Genomic DNA. Translation: BAB03327.2.
AP009324 Genomic DNA. Translation: BAF77456.1.
RefSeqiWP_001100835.1. NC_009782.1.

3D structure databases

ProteinModelPortaliQ9KWK5.
SMRiQ9KWK5. Positions 8-446.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF77456; BAF77456; SAHV_0573.
KEGGisaw:SAHV_0573.
PATRICi19556115. VBIStaAur127830_0578.

Phylogenomic databases

HOGENOMiHOG000279836.
OMAiWFESVCK.
OrthoDBiEOG64FKGZ.

Enzyme and pathway databases

BioCyciSAUR418127:GJP9-590-MONOMER.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the up- and down-regulated genes in vancomycin-resistant Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential hybridization method."
    Kuroda M., Kuwahara-Arai K., Hiramatsu K.
    Biochem. Biophys. Res. Commun. 269:485-490(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VANCOMYCIN RESISTANCE.
  2. "Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
    Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
    Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu3 / ATCC 700698.

Entry informationi

Entry nameiVRAA_STAA1
AccessioniPrimary (citable) accession number: Q9KWK5
Secondary accession number(s): A7WZ14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 4, 2007
Last modified: March 16, 2016
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

May contribute to vancomycin resistance.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.