ID A0A1Q4W4N7_9ACTN Unreviewed; 683 AA.
AC A0A1Q4W4N7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alkyl/aryl-sulfatase {ECO:0000313|EMBL:OKI05038.1};
GN ORFNames=A6A06_10235 {ECO:0000313|EMBL:OKI05038.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI05038.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI05038.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI05038.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKI05038.1}.
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DR EMBL; LWKZ01000012; OKI05038.1; -; Genomic_DNA.
DR RefSeq; WP_073761804.1; NZ_LWKZ01000012.1.
DR AlphaFoldDB; A0A1Q4W4N7; -.
DR STRING; 1718985.A6A06_10235; -.
DR OrthoDB; 5240502at2; -.
DR Proteomes; UP000185893; Unassembled WGS sequence.
DR GO; GO:0018741; F:linear primary-alkylsulfatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0018909; P:dodecyl sulfate metabolic process; IEA:InterPro.
DR CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR Gene3D; 1.25.40.880; Alkyl sulfatase, dimerisation domain; 1.
DR Gene3D; 3.60.15.30; Metallo-beta-lactamase domain; 1.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR InterPro; IPR029229; Alkyl_sulf_C.
DR InterPro; IPR029228; Alkyl_sulf_dimr.
DR InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR PANTHER; PTHR43223; ALKYL/ARYL-SULFATASE; 1.
DR PANTHER; PTHR43223:SF1; ALKYL_ARYL-SULFATASE BDS1; 1.
DR Pfam; PF14864; Alkyl_sulf_C; 1.
DR Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 115..359
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74330 MW; CB5098D0F2D98AA3 CRC64;
MPSEYTEPVE ISPSVAEANR KAAEGSPADG AQDFEDANRQ LLAPPDVPAV YSRTDSSKPV
WNFAAYDFLT DGGEQPPAEV NASLWRQGTL TATAGLFLVV SSSSRAVYQV RGYDLSNMTI
IEGDSGIIVI DPLACYETAQ AALRLYRDTT GNRTPVVGLI YTHSHVDHFG GARGLFAERN
DEVPDGLPVI APDGFLEHAV SENVYAGPAM SRRAEYMYAA NLDKSPHAQV GSGLGLTVST
GEVTLLPPTD SIGAAQAVTS DDWSPADVIP WRKGLHRRVI DGVRLLFQLT PGTEAPAEMN
IYLPELRALC MAENATHTLH NILSLRGAEV RDAHAWATYL TDAIQTFGEQ TEVEFASHHW
PRWGKESILE FLSNQRDMYA YLNDQTLRLI NRGYTGSEIA EELQHLPAGL AEHWYTQGYY
GSLSHNFKAV YQRYMGWFDG NPARLWNLPP TEAGTRYVAA MGGAEAVVQK AQETYDSHDG
DPQAYRWVVE LLDHVIFADP ATVSEQAAKD AKALQIKTFT QLGYGAENGP WRNFFLTGAD
ELRSGPQRPA SAGAPDLVHS MTLEQVFAAL ARSVDGPTAA REQRAAIVLQ WHFTDTGQEC
TSTLRNGVLV YVAGKDLYAG KPQATITLTR AAFDSVLLAG PLFQQNFDAA VTSGAVQVDD
LAAADTVFGY LTVPDPSFPI VTP
//
