ID A0A0J6VW45_MYCCU Unreviewed; 624 AA.
AC A0A0J6VW45;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Metallo-beta-lactamase superfamily protein {ECO:0000313|EMBL:KMO73617.1};
GN ORFNames=MCHUDSM44219_04191 {ECO:0000313|EMBL:KMO73617.1};
OS Mycolicibacterium chubuense (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1800 {ECO:0000313|EMBL:KMO73617.1, ECO:0000313|Proteomes:UP000036176};
RN [1] {ECO:0000313|EMBL:KMO73617.1, ECO:0000313|Proteomes:UP000036176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44219 {ECO:0000313|EMBL:KMO73617.1,
RC ECO:0000313|Proteomes:UP000036176};
RX PubMed=26079817; DOI=10.1093/gbe/evv111;
RA Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S.,
RA Bhattacharya A., Kirsebom L.A.;
RT "Characterization of Three Mycobacterium spp. with Potential Use in
RT Bioremediation by Genome Sequencing and Comparative Genomics.";
RL Genome Biol. Evol. 7:1871-1886(2015).
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:KMO73617.1}.
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DR EMBL; JYNX01000059; KMO73617.1; -; Genomic_DNA.
DR RefSeq; WP_048420103.1; NZ_UATB01000015.1.
DR AlphaFoldDB; A0A0J6VW45; -.
DR PATRIC; fig|1800.3.peg.4216; -.
DR OrthoDB; 5240502at2; -.
DR Proteomes; UP000036176; 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:UP000036176};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 101..323
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 624 AA; 68291 MW; 90AABF78B56764C4 CRC64;
MEHKPPTPTI EAAHRAHLGS LPFDDTRDFA DADRGFIAAQ QPCVITAADG RVVWDNDVYD
FLHGDAPTTV HPSLWRQSQL VAKQGLYEVV EGIYQVRGFD LSNITFVEGD TGIIVIDPLV
STEVAAAALA LYRRHRGERT VVAVIYTHSH VDHFGGVLGV TSQADVDAGK VAVLAPEGFT
EHAVQENVYA GTAMARRAGY MYGAVLERGP QGQVGCGLGQ TPSTGEVAII VPTVDIRETG
ETHTIDGVQI EFQMAPGTEA PAEMHFYFPK YRALCMAENA THNLHNLLTL RGALVRDPHG
WAGYLTEAID TFADRADVVF ASHHWPTWGK ERIVEFLSLQ RDLYAYLHDQ TLRQLNQGYT
GIEIAETFAM PPALERAWHA HGYYGSVSHN VKAVYQRYMG WFDGNPGRLW PHPPEAIGPR
YVAAMGGIDR VVELAQQAFD DGDFRWAATL LDHAIFTDEN HASARQLYAD TLEQLAYGSE
TATWRNFFLA GATELRDGNF GTPTTTSTTM AAQLSPEQMF DVLAISVNGP RAWDLDLAID
VTFEDTATNY RLTLRNGVLV YRKVDADDQT AQATIQLATK VRLLSLAAGD ATSPGVEITG
DGEVLTALVG VLDKPDPGFD IVTP
//