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Database: UniProt
Entry: A0A4R8RFU1_9MYCO
LinkDB: A0A4R8RFU1_9MYCO
Original site: A0A4R8RFU1_9MYCO 
ID   A0A4R8RFU1_9MYCO        Unreviewed;       631 AA.
AC   A0A4R8RFU1;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Metallo-beta-lactamase superfamily protein {ECO:0000313|EMBL:TDZ52087.1};
GN   ORFNames=CCUG63697_00558 {ECO:0000313|EMBL:TDZ52087.1};
OS   Mycobacteroides franklinii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides.
OX   NCBI_TaxID=948102 {ECO:0000313|EMBL:TDZ52087.1, ECO:0000313|Proteomes:UP000295165};
RN   [1] {ECO:0000313|EMBL:TDZ52087.1, ECO:0000313|Proteomes:UP000295165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 63697 {ECO:0000313|EMBL:TDZ52087.1,
RC   ECO:0000313|Proteomes:UP000295165};
RX   PubMed=30872669; DOI=.1038/s41598-019-40922-x;
RA   Behra P.R., Das S., Pettersson B.M., Shirreff L., DuCote T.,
RA   Jacobsson K.G., Ennis D.G., Kirsebom L.A.;
RT   "Extended insight into the Mycobacterium chelonae-abscessus complex through
RT   whole genome sequencing of Mycobacterium salmoniphilum outbreak and
RT   Mycobacterium salmoniphilum-like strains.";
RL   Sci. Rep. 9:4603-4603(2019).
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:TDZ52087.1}.
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DR   EMBL; PECC01000026; TDZ52087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R8RFU1; -.
DR   Proteomes; UP000295165; 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:UP000295165};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          102..324
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   631 AA;  68894 MW;  F9450A3BEE8FC96B CRC64;
     MPEQTQPTSR IIDQNAAAAQ ELPFASTVDQ ADADRGFIAA LEPGVVTDAA GKTVWDNDSY
     SFLGDSCPAS VHPSLWRQCG LNIRQGLYLV TEGIYQVRGL DISNMTIVEG ENGVIVIDPL
     VSAETAAAAL ALYRSHRGDR PVTGLIYTHS HADHFGGALG VVSTEDVAAG RCPVLAPAGF
     LEHAVAENVY AGTAMTRRAV YMYGAVLPRG PLGQVGSGLG QTNSIGTVTL IPPTLDITHT
     GQEETIDGVR MIFQLTPGTE APAEMNFHFP QHRALCMAEN ATHTLHNLLT LRGALVRDPH
     VWARYITEAI NLYAHDADVV FASHHWPTWD TARLVEYLSL QRDLYAYLHD QTLRQLNQGF
     VGSEIAETLQ LPPAIAGAWH ARGYYGSISH NVKAIYQRYM GWFDGNPAHL WEHPPVANAQ
     RHVEFMGGSE EVLRKAHIAF EEGDYRWVAQ VVNYVIFADP ANEAAKMLQA SCFEQLGYGA
     ENATWRNFYL MGAYELRHGN VGTPMAVGSP TMMAALTVDQ VFDALSLRIN GPKAWNERFV
     SDWTFTDEDR VHRVELRNGV LVHYDRPAGI SPPDVTFTLT RPTLIDVLLD GKDPAQLVAS
     GEIAVEGDLT GLARLVAVLD APDPGFAIVT P
//
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