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Protein

Lactonase drp35

Gene

drp35

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity).By similarity

Cofactori

Ca2+1 PublicationNote: Binds 2 Ca2+ ions per subunit.1 Publication

pH dependencei

Optimum pH is about 6.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Calcium 1; catalytic1
Metal bindingi109Calcium 2; via carbonyl oxygen1
Metal bindingi111Calcium 2; via carbonyl oxygen1
Metal bindingi129Calcium 2; via carbonyl oxygen1
Metal bindingi132Calcium 2; via carbonyl oxygen1
Metal bindingi134Calcium 2; via carbonyl oxygen1
Metal bindingi137Calcium 1; catalytic1
Metal bindingi184Calcium 1; catalytic1
Active sitei235Proton donorSequence analysis1
Metal bindingi235Calcium 1; catalytic1
Metal bindingi236Calcium 1; catalytic1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lactonase drp35 (EC:3.1.1.-)
Gene namesi
Name:drp35
Ordered Locus Names:SAV2688
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47E → A: Loss of activity. 1 Publication1
Mutagenesisi47E → Q: Loss of activity due to inability to bind calcium ion. 1 Publication1
Mutagenesisi47E → S: Loss of activity. 1 Publication1
Mutagenesisi63F → A: 2.5-fold increase in lactonase activity. 1 Publication1
Mutagenesisi92K → A: Increase in lactonase activity. 1 Publication1
Mutagenesisi137D → A: Loss of activity. 1 Publication1
Mutagenesisi137D → N: Loss of activity but still able to bind calcium ion. 1 Publication1
Mutagenesisi137D → S: Loss of activity. 1 Publication1
Mutagenesisi138D → A: Decrease in lactonase activity. 1 Publication1
Mutagenesisi151D → A: Decrease in lactonase activity. 1 Publication1
Mutagenesisi184N → A: Loss of activity. 1 Publication1
Mutagenesisi184N → D: Decrease in lactonase activity. 1 Publication1
Mutagenesisi184N → S: Loss of activity. 1 Publication1
Mutagenesisi185G → A: Decrease in lactonase activity. 1 Publication1
Mutagenesisi235D → A: Loss of activity. 1 Publication1
Mutagenesisi235D → N: Loss of activity due to inability to bind calcium ion. 1 Publication1
Mutagenesisi235D → S: Loss of activity. 1 Publication1
Mutagenesisi236S → A: Decrease in lactonase activity. 1 Publication1
Mutagenesisi237C → A: Increase in lactonase activity. 1 Publication1
Mutagenesisi280R → A: Increase in lactonase activity. 1 Publication1
Mutagenesisi301E → A: Increase in lactonase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002597491 – 324Lactonase drp35Add BLAST324

Proteomic databases

PaxDbiQ99QV3.

2D gel databases

World-2DPAGE0002:Q99QV3.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV2688.

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 17Combined sources4
Helixi25 – 27Combined sources3
Beta strandi30 – 32Combined sources3
Beta strandi34 – 42Combined sources9
Beta strandi46 – 51Combined sources6
Beta strandi57 – 61Combined sources5
Turni62 – 64Combined sources3
Beta strandi66 – 70Combined sources5
Turni72 – 74Combined sources3
Beta strandi77 – 82Combined sources6
Beta strandi84 – 93Combined sources10
Beta strandi99 – 103Combined sources5
Beta strandi107 – 109Combined sources3
Beta strandi112 – 116Combined sources5
Beta strandi124 – 127Combined sources4
Beta strandi129 – 132Combined sources4
Beta strandi136 – 141Combined sources6
Beta strandi147 – 151Combined sources5
Beta strandi161 – 166Combined sources6
Beta strandi173 – 188Combined sources16
Beta strandi192 – 199Combined sources8
Helixi200 – 202Combined sources3
Beta strandi204 – 210Combined sources7
Beta strandi214 – 227Combined sources14
Beta strandi230 – 240Combined sources11
Beta strandi245 – 250Combined sources6
Turni251 – 253Combined sources3
Beta strandi254 – 258Combined sources5
Beta strandi264 – 269Combined sources6
Helixi273 – 275Combined sources3
Beta strandi283 – 286Combined sources4
Beta strandi292 – 298Combined sources7
Helixi300 – 302Combined sources3
Beta strandi306 – 312Combined sources7
Helixi321 – 323Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DG0X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L2-324[»]
2DG1X-ray1.72A/B/C/D/E/F2-324[»]
2DSOX-ray2.10A/B/C/D/E/F2-324[»]
ProteinModelPortaliQ99QV3.
SMRiQ99QV3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99QV3.

Family & Domainsi

Sequence similaritiesi

Belongs to the SMP-30/CGR1 family.Curated

Phylogenomic databases

eggNOGiENOG4108TY5. Bacteria.
COG3386. LUCA.
HOGENOMiHOG000280331.
KOiK02352.
OMAiPIGQILM.
PhylomeDBiQ99QV3.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR013658. SGL.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99QV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSQQDLPTL FYSGKSNSAV PIISESELQT ITAEPWLEIS KKGLQLEGLN
60 70 80 90 100
FDRQGQLFLL DVFEGNIFKI NPETKEIKRP FVSHKANPAA IKIHKDGRLF
110 120 130 140 150
VCYLGDFKST GGIFAATENG DNLQDIIEDL STAYCIDDMV FDSKGGFYFT
160 170 180 190 200
DFRGYSTNPL GGVYYVSPDF RTVTPIIQNI SVANGIALST DEKVLWVTET
210 220 230 240 250
TANRLHRIAL EDDGVTIQPF GATIPYYFTG HEGPDSCCID SDDNLYVAMY
260 270 280 290 300
GQGRVLVFNK RGYPIGQILI PGRDEGHMLR STHPQFIPGT NQLIICSNDI
310 320
EMGGGSMLYT VNGFAKGHQS FQFQ
Length:324
Mass (Da):35,964
Last modified:June 1, 2001 - v1
Checksum:iA2C94FCB38F2F4AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58850.1.
RefSeqiWP_000987672.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58850; BAB58850; SAV2688.
GeneIDi28379666.
KEGGisav:SAV2688.
PATRICi19566318. VBIStaAur52173_2785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58850.1.
RefSeqiWP_000987672.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DG0X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L2-324[»]
2DG1X-ray1.72A/B/C/D/E/F2-324[»]
2DSOX-ray2.10A/B/C/D/E/F2-324[»]
ProteinModelPortaliQ99QV3.
SMRiQ99QV3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV2688.

2D gel databases

World-2DPAGE0002:Q99QV3.

Proteomic databases

PaxDbiQ99QV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58850; BAB58850; SAV2688.
GeneIDi28379666.
KEGGisav:SAV2688.
PATRICi19566318. VBIStaAur52173_2785.

Phylogenomic databases

eggNOGiENOG4108TY5. Bacteria.
COG3386. LUCA.
HOGENOMiHOG000280331.
KOiK02352.
OMAiPIGQILM.
PhylomeDBiQ99QV3.

Miscellaneous databases

EvolutionaryTraceiQ99QV3.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR013658. SGL.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDRP35_STAAM
AccessioniPrimary (citable) accession number: Q99QV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.