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Database: UniProt
Entry: A0A085U7L1_YERRU
LinkDB: A0A085U7L1_YERRU
Original site: A0A085U7L1_YERRU 
ID   A0A085U7L1_YERRU        Unreviewed;       708 AA.
AC   A0A085U7L1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 42.
DE   SubName: Full=Alkyl sulfatase {ECO:0000313|EMBL:CEK27558.1};
DE            EC=3.1.6.- {ECO:0000313|EMBL:CEK27558.1};
GN   ORFNames=CSF007_9025 {ECO:0000313|EMBL:CEK27558.1};
OS   Yersinia ruckeri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=29486 {ECO:0000313|EMBL:CEK27558.1};
RN   [1] {ECO:0000313|EMBL:CEK27558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK27558.1};
RA   Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT   "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82, Etiologic
RT   Agent of Red Mouth Disease in Salmonid Fish.";
RL   Genome Announc. 3:1-2(2015).
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC       sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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DR   EMBL; LN681231; CEK27558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085U7L1; -.
DR   PATRIC; fig|29486.44.peg.1449; -.
DR   OMA; AENCTHN; -.
DR   OrthoDB; 9815874at2; -.
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:CEK27558.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..708
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015029293"
FT   DOMAIN          144..366
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   708 AA;  78737 MW;  C2341C349273A19B CRC64;
     MKLSKIAQFT AIIIAANSLN LVYAASDGVD VYANSDTEHF HPQGKPPSKY TIDLYNQVKK
     SLPFEDTRDF EESQKGLIAK PPFKQIMADA GNVAWDMGSY EFLLQGKDFP SINPSLQRQA
     VLNMAYGLYE VLPDRIYQVR GFDLANMTLI KGDTGWIIFD PLTAKETAAA ALAFANEKLG
     NRPVVAVVFS HSHVDHFGGV RGVVDEKDVQ SGKVPIIAPE HFMQAAISEN VFSGNAMARR
     VQYQYGVLLD RSPFGHVDQA IGKNIANGNT GLIAPTRFIT KDFEEITIDG VKMVFQNTPD
     TEAPAEMNTY FPQFKAFWAA ENVTGTIHNI YTLRGAEIRN ALNWSKQINN ALYKFGDDVQ
     VMFASHSWPR WGNERIQEVL RAQRDLYANM NNQVLHYANQ GVTINEIQNV YQAPPSLQRQ
     WAARSYHGSE GHNTRGIINR YLGYWDGNPA TLVPLSPRES APLYVEMMGG AAKILAKGKQ
     LNDQGKYLEA TEILNKLVYA EPKNQEARNM LADAFEQLGY QKESTSVRNS FLQAAYELRT
     GLPNALAPKA TGPDVIRALP TALWLDFLAI SMDSQRADGM NFTINLITPD NNEKYLIEMS
     NATLTNIADY QAKKPTLTIT VNRSDLNSVM MGISTFEELE AAGKAKFEGD RTAYDKLKST
     LVKFTPNFEI MPGTLNASPT PASGNTNNTA PTYNVKPFEY VIYSAEED
//
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