ID   F2RLQ3_STRVP            Unreviewed;       684 AA.
AC   F2RLQ3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Alkyl sulfatase {ECO:0000313|EMBL:CCA60433.1};
DE            EC=3.1.6.- {ECO:0000313|EMBL:CCA60433.1};
GN   OrderedLocusNames=SVEN_7147 {ECO:0000313|EMBL:CCA60433.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA60433.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA60433.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA60433.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC       sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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DR   EMBL; FR845719; CCA60433.1; -; Genomic_DNA.
DR   RefSeq; WP_015038328.1; NZ_JABVZO010000191.1.
DR   AlphaFoldDB; F2RLQ3; -.
DR   STRING; 953739.SVEN_7147; -.
DR   GeneID; 69869127; -.
DR   KEGG; sve:SVEN_7147; -.
DR   PATRIC; fig|953739.5.peg.2373; -.
DR   eggNOG; COG2015; Bacteria.
DR   HOGENOM; CLU_014655_1_0_11; -.
DR   OrthoDB; 5240502at2; -.
DR   Proteomes; UP000006854; Chromosome.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCA60433.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          167..386
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  73883 MW;  421D47BEF3C0A97C CRC64;
     MTPMNRRGFV AAAAAMGAAA ASVSLNPQTA QALAGHLPRA MGTPTRTDGL PYDDETDFGD
     ADRGFVAAFT GGPITDATGR TVWDPGAYRF LTEAEDAREG RGDDGSGRGG DGGGHGGDGR
     PGADGDDGGH AGPATVDPSL WRQARLLSRQ GLYRVTDRIY QVRGLDLSNM TIVEGDTGII
     VIDPLISAET AAAALRLYRT HRGDRAVRAM IYTHPHVDHF GGCRGVLPDG AGDVPVLAPK
     GFMEHAVSEN VYVGTAMARR AGYMYGSTLP KNAAAQVGCG LGLTVSLGTV GLIAPTRYIG
     ATGEEVVLDG VRIRFQMTPG TECQEEMNFL FPDLRAVCMA ENATHTMHNI LTLRGAQVRD
     AHAWAGYLTE SIGLYDGAAD VAFASHHWPT WGNDAIVALL THQRDLYGYL HDQTVRLINR
     GLTGTEIAET FRLPPQLEGV WANRGYYGSL SHNVKAVYQR YMGWFDGNPA HLWEHPPAEE
     ARLYVESLGG QAAVRARARH YADRGELRFA VTLLNHAVFN DPRDSRAKRQ LAALYTRLGQ
     AVENAVWRNF YLTGAQELLH GITPRATATL GPDMYLALTV GQIIDSLAVR VDGPKAWSLR
     IVMDWHIGAD YWHLRLANGL LTWTRDDRPA ADAALTLRMT KPQLLTLLAG KGTAGITMTG
     DRGLLPRLLA VLETPEPDFP IVTP
//