ID A0A418WNU5_9SPHN Unreviewed; 648 AA.
AC A0A418WNU5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:RJF92901.1};
GN ORFNames=D3876_00470 {ECO:0000313|EMBL:RJF92901.1};
OS Sphingomonas cavernae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2320861 {ECO:0000313|EMBL:RJF92901.1, ECO:0000313|Proteomes:UP000286100};
RN [1] {ECO:0000313|EMBL:RJF92901.1, ECO:0000313|Proteomes:UP000286100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2R01-6 {ECO:0000313|EMBL:RJF92901.1,
RC ECO:0000313|Proteomes:UP000286100};
RA Zhu H.;
RL Submitted (SEP-2018) 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:RJF92901.1}.
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DR EMBL; QYUM01000002; RJF92901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418WNU5; -.
DR OrthoDB; 9815874at2; -.
DR Proteomes; UP000286100; 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:RJF92901.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286100};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..648
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019050026"
FT DOMAIN 122..344
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 648 AA; 69809 MW; CB26D2F9BB0F0550 CRC64;
MKKICIALLL GGAGTAVLAQ DVSSKPASAS TKAANRQIID GLDMGDRRDE TFSTRGFVAT
RTDPVIRAAD GGVAWDLSRY DWVKGDAPDT VNASLWRQMK LLKAHGLYKL TEGVWQVRGF
DISNMTVIKG RTGWILIDPL LGQETARAAL DLVNANLGNR PVTAVIYTHS HGDHFGGVRG
VVDEADVTAG KVAIVAPDRL IEEAIAENVI AGNAMGRRAT YQFGSALTPG ERGQMGSGIG
PGTSAGGITL LAPTDLVKAT GDTRTIDGVT FEFQMVPESE APSEFNLYLP AQKALIIGEI
AVPTLHNIQT PRGALVRDAL KWAGYLTQAV RLYGDRSDVV AASHGWPRFG QNEVKQYLTL
QRDNYKFLHD QSVRLMNAGL TAEEIAETIT PPPVIARQWF NRGYYGTYSH NSKAVYHRYM
GWYDGVPAHL DPLPPVEVGK RYVAAIGGQA QVLTLGRAAI RAGDYRWAGE LLNHLVSAEP
ANGDARALLA DAYEQLGYQA ESAIWRNMYL MGALELRGKP DAPSRLQGLD LLRATPTPML
LDAIATRLNP AVIGDRAMTL NLVFTDRKER ALISVRNAVL VPEMDQAEAS PTATLTGPRA
LFLGLFFQKT PVAQLESAGL KVTGDKAAIT ALQAALQAPD PGFAIVTP
//
