SULF_CLOP1
ID SULF_CLOP1 Reviewed; 481 AA.
AC Q0TUK6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Arylsulfatase;
DE EC=3.1.6.1;
DE AltName: Full=Cys-type sulfatase;
GN OrderedLocusNames=CPF_0221;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [2]
RP FUNCTION, KINETIC PARAMETERS, IDENTIFICATION BY MASS SPECTROMETRY,
RP OXOALANINE AT CYS-51, AND OXIDATION BY ANSME.
RX PubMed=16766528; DOI=10.1074/jbc.m602504200;
RA Berteau O., Guillot A., Benjdia A., Rabot S.;
RT "A new type of bacterial sulfatase reveals a novel maturation pathway in
RT prokaryotes.";
RL J. Biol. Chem. 281:22464-22470(2006).
RN [3]
RP OXIDATION BY ANSME.
RX PubMed=17335281; DOI=10.1021/ja067175e;
RA Benjdia A., Leprince J., Guillot A., Vaudry H., Rabot S., Berteau O.;
RT "Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to
RT catalyze in vitro sulfatase post-translational modification.";
RL J. Am. Chem. Soc. 129:3462-3463(2007).
CC -!- FUNCTION: Has sulfatase activity toward para-nitrophenyl sulfate, which
CC is increased in presence of calcium ion. {ECO:0000269|PubMed:16766528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38 mM for para-nitrophenyl sulfate {ECO:0000269|PubMed:16766528};
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity (By
CC similarity). This conversion can be carried out in vitro by AnSME under
CC anaerobic conditions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; CP000246; ABG83206.1; -; Genomic_DNA.
DR RefSeq; WP_011590105.1; NC_008261.1.
DR AlphaFoldDB; Q0TUK6; -.
DR SMR; Q0TUK6; -.
DR STRING; 195103.CPF_0221; -.
DR EnsemblBacteria; ABG83206; ABG83206; CPF_0221.
DR GeneID; 29572654; -.
DR KEGG; cpf:CPF_0221; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_2_9; -.
DR OMA; DHGELHG; -.
DR OrthoDB; 1067869at2; -.
DR SABIO-RK; Q0TUK6; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Oxidation.
FT CHAIN 1..481
FT /note="Arylsulfatase"
FT /id="PRO_0000273380"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16766528"
FT ACT_SITE 102
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:16766528"
SQ SEQUENCE 481 AA; 55801 MW; 3B55B0CF39602318 CRC64;
MKPNIVLIMV DQMRGDCLGV NGNEFIETPN LDMMATEGYN FENAYTAVPS CIASRASILT
GMSQKSHGRV GYEDGVSWNY ENTIASEFSK AGYHTQCIGK MHVYPERNLC GFHNIMLHDG
YLHFARNKEG KASTQIEQCD DYLKWFREKK GHNVDLIDIG LDCNSWVSRP WGYEENLHPT
NWVVNESIDF LRRKDPSKPF FLKMSFVRPH SPLDPPKFYF DMYKDEDLPE PLMGDWANKE
DEENRGKDIN CVKGIINKKA LKRAKAAYYG SITHIDHQIG RFLIALSEYG ELNNTIFLFV
SDHGDMMGDH NWFRKGIPYE GSSRVPFFIY DPGNLLKGKK GKVFDEVLEL RDIMPTLLDF
AHISIPDSVE GLSLKNLIEE RNSTWRDYIH GEHSFGEDSN HYIVTKRDKF LWFSQRGEEQ
YFDLENDPKE LTNLIDSEEY KERIDYLRKI LIKELEGREE GYTDGNRLLK GHPVSTLKHI
R
