DRP35_STAAN
ID DRP35_STAAN Reviewed; 324 AA.
AC Q7A338;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Lactonase drp35;
DE EC=3.1.1.-;
GN Name=drp35; OrderedLocusNames=SA2480;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, COFACTOR, INDUCTION, REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=16019162; DOI=10.1016/j.femsle.2005.06.038;
RA Morikawa K., Hidaka T., Murakami H., Hayashi H., Ohta T.;
RT "Staphylococcal Drp35 is the functional counterpart of the eukaryotic
RT PONs.";
RL FEMS Microbiol. Lett. 249:185-190(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- FUNCTION: Exhibits lactonase activity for dihydrocoumarin or 2-
CC coumaranone, although its natural substrate is not known. Acts in cells
CC with perturbed membrane integrity and is possibly related to the
CC membrane homeostasis. Contributes to bacitracin resistance.
CC {ECO:0000269|PubMed:16019162}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16019162};
CC Note=Binds 2 Ca(2+) ions per subunit. {ECO:0000269|PubMed:16019162};
CC -!- ACTIVITY REGULATION: Activity is decreased by EGTA or EDTA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16019162}.
CC -!- INDUCTION: Induced by cell wall-affecting antibiotics such as
CC oxacillin, beta-lactams, vancomycin, fosfomycin, bacitracin and
CC detergents such as Triton X-100, SDS, Nonidet P40, and CHAPS.
CC {ECO:0000269|PubMed:16019162}.
CC -!- MISCELLANEOUS: Not essential for cells to maintain the levels of
CC resistance to most of the cell wall-affecting antibiotics although they
CC can effectively induce its expression.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR EMBL; BA000018; BAB43786.1; -; Genomic_DNA.
DR PIR; H90077; H90077.
DR AlphaFoldDB; Q7A338; -.
DR SMR; Q7A338; -.
DR SWISS-2DPAGE; Q7A338; -.
DR EnsemblBacteria; BAB43786; BAB43786; BAB43786.
DR KEGG; sau:SA2480; -.
DR HOGENOM; CLU_036110_2_0_9; -.
DR OMA; VWVLNHR; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR013658; SGL.
DR Pfam; PF08450; SGL; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Calcium; Cytoplasm; Hydrolase; Metal-binding.
FT CHAIN 1..324
FT /note="Lactonase drp35"
FT /id="PRO_0000259751"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 35964 MW; A2C94FCB38F2F4AC CRC64;
MMSQQDLPTL FYSGKSNSAV PIISESELQT ITAEPWLEIS KKGLQLEGLN FDRQGQLFLL
DVFEGNIFKI NPETKEIKRP FVSHKANPAA IKIHKDGRLF VCYLGDFKST GGIFAATENG
DNLQDIIEDL STAYCIDDMV FDSKGGFYFT DFRGYSTNPL GGVYYVSPDF RTVTPIIQNI
SVANGIALST DEKVLWVTET TANRLHRIAL EDDGVTIQPF GATIPYYFTG HEGPDSCCID
SDDNLYVAMY GQGRVLVFNK RGYPIGQILI PGRDEGHMLR STHPQFIPGT NQLIICSNDI
EMGGGSMLYT VNGFAKGHQS FQFQ
