DRP35_STAAM
ID DRP35_STAAM Reviewed; 324 AA.
AC Q99QV3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Lactonase drp35;
DE EC=3.1.1.-;
GN Name=drp35; OrderedLocusNames=SAV2688;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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 X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-324 OF APOPROTEIN; COMPLEX WITH
RP CALCIUM IONS AND MUTANT ASN-137, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP REACTION MECHANISM, AND MUTAGENESIS OF GLU-47; PHE-63; LYS-92; ASP-137;
RP ASP-138; ASP-151; ASN-184; GLY-185; ASP-235; SER-236; CYS-237; ARG-280 AND
RP GLU-301.
RX PubMed=17166853; DOI=10.1074/jbc.m607340200;
RA Tanaka Y., Morikawa K., Ohki Y., Yao M., Tsumoto K., Watanabe N., Ohta T.,
RA Tanaka I.;
RT "Structural and mutational analyses of drp35 from Staphylococcus aureus: a
RT possible mechanism for its lactonase activity.";
RL J. Biol. Chem. 282:5770-5780(2007).
CC -!- FUNCTION: Exhibits lactonase activity. Acts in cells with perturbed
CC membrane integrity and is possibly related to the membrane homeostasis
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17166853};
CC Note=Binds 2 Ca(2+) ions per subunit. {ECO:0000269|PubMed:17166853};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 6.0. {ECO:0000269|PubMed:17166853};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR EMBL; BA000017; BAB58850.1; -; Genomic_DNA.
DR PDB; 2DG0; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=2-324.
DR PDB; 2DG1; X-ray; 1.72 A; A/B/C/D/E/F=2-324.
DR PDB; 2DSO; X-ray; 2.10 A; A/B/C/D/E/F=2-324.
DR PDBsum; 2DG0; -.
DR PDBsum; 2DG1; -.
DR PDBsum; 2DSO; -.
DR AlphaFoldDB; Q99QV3; -.
DR SMR; Q99QV3; -.
DR World-2DPAGE; 0002:Q99QV3; -.
DR PaxDb; Q99QV3; -.
DR EnsemblBacteria; BAB58850; BAB58850; SAV2688.
DR KEGG; sav:SAV2688; -.
DR HOGENOM; CLU_036110_2_0_9; -.
DR OMA; VWVLNHR; -.
DR PhylomeDB; Q99QV3; -.
DR EvolutionaryTrace; Q99QV3; -.
DR Proteomes; UP000002481; 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 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 3D-structure; Calcium; Cytoplasm; Hydrolase; Metal-binding.
FT CHAIN 1..324
FT /note="Lactonase drp35"
FT /id="PRO_0000259749"
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 BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT MUTAGEN 47
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 47
FT /note="E->Q: Loss of activity due to inability to bind
FT calcium ion."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 47
FT /note="E->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 63
FT /note="F->A: 2.5-fold increase in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 92
FT /note="K->A: Increase in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 137
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 137
FT /note="D->N: Loss of activity but still able to bind
FT calcium ion."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 137
FT /note="D->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 138
FT /note="D->A: Decrease in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 151
FT /note="D->A: Decrease in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 184
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 184
FT /note="N->D: Decrease in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 184
FT /note="N->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 185
FT /note="G->A: Decrease in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 235
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 235
FT /note="D->N: Loss of activity due to inability to bind
FT calcium ion."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 235
FT /note="D->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 236
FT /note="S->A: Decrease in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 237
FT /note="C->A: Increase in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 280
FT /note="R->A: Increase in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT MUTAGEN 301
FT /note="E->A: Increase in lactonase activity."
FT /evidence="ECO:0000269|PubMed:17166853"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:2DG1"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2DG1"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2DG1"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 173..188
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2DG1"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 214..227
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2DG1"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:2DG1"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:2DG1"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2DG1"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:2DG1"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2DG1"
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
