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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium 1; catalytic
Metal bindingi109 – 1091Calcium 2; via carbonyl oxygen
Metal bindingi111 – 1111Calcium 2; via carbonyl oxygen
Metal bindingi129 – 1291Calcium 2; via carbonyl oxygen
Metal bindingi132 – 1321Calcium 2; via carbonyl oxygen
Metal bindingi134 – 1341Calcium 2; via carbonyl oxygen
Metal bindingi137 – 1371Calcium 1; catalytic
Metal bindingi184 – 1841Calcium 1; catalytic
Active sitei235 – 2351Proton donorSequence analysis
Metal bindingi235 – 2351Calcium 1; catalytic
Metal bindingi236 – 2361Calcium 1; catalytic

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-2756-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471E → A: Loss of activity. 1 Publication
Mutagenesisi47 – 471E → Q: Loss of activity due to inability to bind calcium ion. 1 Publication
Mutagenesisi47 – 471E → S: Loss of activity. 1 Publication
Mutagenesisi63 – 631F → A: 2.5-fold increase in lactonase activity. 1 Publication
Mutagenesisi92 – 921K → A: Increase in lactonase activity. 1 Publication
Mutagenesisi137 – 1371D → A: Loss of activity. 1 Publication
Mutagenesisi137 – 1371D → N: Loss of activity but still able to bind calcium ion. 1 Publication
Mutagenesisi137 – 1371D → S: Loss of activity. 1 Publication
Mutagenesisi138 – 1381D → A: Decrease in lactonase activity. 1 Publication
Mutagenesisi151 – 1511D → A: Decrease in lactonase activity. 1 Publication
Mutagenesisi184 – 1841N → A: Loss of activity. 1 Publication
Mutagenesisi184 – 1841N → D: Decrease in lactonase activity. 1 Publication
Mutagenesisi184 – 1841N → S: Loss of activity. 1 Publication
Mutagenesisi185 – 1851G → A: Decrease in lactonase activity. 1 Publication
Mutagenesisi235 – 2351D → A: Loss of activity. 1 Publication
Mutagenesisi235 – 2351D → N: Loss of activity due to inability to bind calcium ion. 1 Publication
Mutagenesisi235 – 2351D → S: Loss of activity. 1 Publication
Mutagenesisi236 – 2361S → A: Decrease in lactonase activity. 1 Publication
Mutagenesisi237 – 2371C → A: Increase in lactonase activity. 1 Publication
Mutagenesisi280 – 2801R → A: Increase in lactonase activity. 1 Publication
Mutagenesisi301 – 3011E → A: Increase in lactonase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Lactonase drp35PRO_0000259749Add
BLAST

Proteomic databases

PaxDbiQ99QV3.

2D gel databases

World-2DPAGE0002:Q99QV3.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV2688.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 174Combined sources
Helixi25 – 273Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 429Combined sources
Beta strandi46 – 516Combined sources
Beta strandi57 – 615Combined sources
Turni62 – 643Combined sources
Beta strandi66 – 705Combined sources
Turni72 – 743Combined sources
Beta strandi77 – 826Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi173 – 18816Combined sources
Beta strandi192 – 1998Combined sources
Helixi200 – 2023Combined sources
Beta strandi204 – 2107Combined sources
Beta strandi214 – 22714Combined sources
Beta strandi230 – 24011Combined sources
Beta strandi245 – 2506Combined sources
Turni251 – 2533Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi264 – 2696Combined sources
Helixi273 – 2753Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi292 – 2987Combined sources
Helixi300 – 3023Combined sources
Beta strandi306 – 3127Combined sources
Helixi321 – 3233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-324.
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.
OrthoDBiEOG60919F.
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.
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
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. Positions 4-324.
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.
KEGGisav:SAV2688.
PATRICi19566318. VBIStaAur52173_2785.

Phylogenomic databases

eggNOGiENOG4108TY5. Bacteria.
COG3386. LUCA.
HOGENOMiHOG000280331.
KOiK02352.
OMAiPIGQILM.
OrthoDBiEOG60919F.
PhylomeDBiQ99QV3.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-2756-MONOMER.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  2. "Structural and mutational analyses of drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity."
    Tanaka Y., Morikawa K., Ohki Y., Yao M., Tsumoto K., Watanabe N., Ohta T., Tanaka I.
    J. Biol. Chem. 282:5770-5780(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-324 OF APOPROTEIN; COMPLEX WITH CALCIUM IONS AND MUTANT ASN-137, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, MUTAGENESIS OF GLU-47; PHE-63; LYS-92; ASP-137; ASP-138; ASP-151; ASN-184; GLY-185; ASP-235; SER-236; CYS-237; ARG-280 AND GLU-301.

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: March 16, 2016
This is version 88 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.