ID A0A561UQ85_9ACTN Unreviewed; 637 AA.
AC A0A561UQ85;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alkyl sulfatase BDS1-like metallo-beta-lactamase superfamily hydrolase {ECO:0000313|EMBL:TWG01543.1};
GN ORFNames=FHX73_115444 {ECO:0000313|EMBL:TWG01543.1};
OS Kitasatospora viridis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=281105 {ECO:0000313|EMBL:TWG01543.1, ECO:0000313|Proteomes:UP000317940};
RN [1] {ECO:0000313|EMBL:TWG01543.1, ECO:0000313|Proteomes:UP000317940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44826 {ECO:0000313|EMBL:TWG01543.1,
RC ECO:0000313|Proteomes:UP000317940};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:TWG01543.1}.
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DR EMBL; VIWT01000001; TWG01543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A561UQ85; -.
DR OrthoDB; 5240502at2; -.
DR Proteomes; UP000317940; 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, ECO:0000313|EMBL:TWG01543.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000317940};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 120..339
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 18..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 68480 MW; F957930E0D30CAA2 CRC64;
MTPLHRPDTA GAAAAALAPN PQTAGPGSAT GSTPLNGPDF TDDTDFADAD RGFIAAFTGG
PIRTADGRTA WDPAAYAFLA DGEPAPATAD PSLWRQARLL SRQGLYRVTD RIYQVRGLDL
SNMTIVEGDS GIIVIDPLIS AETAAAALRL YREHRGDRAV RAMIYTHPHV DHFGGCRGVL
PDGAGEVPIL APAGFMEHAV SENLHVGTAM ARRAGYMYGA HLPAGAAAQL GCGLGLTVSL
GTVGLIAPTR YVTATGEEVT LDGVRIRFQL TPGTECQEEM NFLFPDLRAV CMAENATHTM
HNIITLRGAQ VRDARAWAGY LTEAIGLYDG AADVAFASHH WPTWGGERIT ALLTQQRDLY
AYLHDQTVRL INQGRTPAEI AEELQLPPAI ASVWANQGYY GSLSHNVKGI YQRYLGWFDG
NPAHLWELPP VEEARRWVEV LGGNAAVREQ AERYARAGDL RFAVTLLNHA VFNDPDDRAA
RDQLAGLYTT LAHGAENAVW RNFYLTGALE LTEGVQTAQR TGAGIDMFLA LTVGQLLDGL
AVRLNGPRAW DSSLAVDWFV EDAYWHLRLA HGVLTWTTDD RPDPTAGLTM TMTKPQLLGA
LAGLGTEGIT MAGDPGLLTQ LLGLLDAPDP NFAIVTP
//
