ID A0A2K9LKN1_9GAMM Unreviewed; 677 AA.
AC A0A2K9LKN1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|SMART:SM00849};
GN ORFNames=Kalk_10440 {ECO:0000313|EMBL:AUM12810.1};
OS Ketobacter alkanivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM12810.1, ECO:0000313|Proteomes:UP000235116};
RN [1] {ECO:0000313|Proteomes:UP000235116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA Kim S.-J., Rhee S.-K.;
RT "Direct submision.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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DR EMBL; CP022684; AUM12810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9LKN1; -.
DR KEGG; kak:Kalk_10440; -.
DR OrthoDB; 9815874at2; -.
DR Proteomes; UP000235116; 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 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:UP000235116};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 122..344
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 74942 MW; 19032F75E2DA941C CRC64;
MAAGGGGVVT SDPSKHFDPK GKLPSKYTIE LQEGLRKSLP FDDKRDFEEA KRGFIAAPTY
KQIMAEAGNV AWDMGSYEWL LEEGQNFDSI HPSLQRQAIL NMAYGLYEVV PGKIYQVRGY
DLANISFIKG KTGWIVFDPL TAKETAAAAL KFINEQLGER PVVAVVYSHS HGDHFGGVRG
VVDEADVKSG KVKIIAPEGF MHHAVAENVM AGNVMTRRMF FQYGVLLPRS PYGHVDQSIG
KNTAAGNLGL IEPNVIIKQD FEDMTIDGIK MVFQNTPGTE APAEMNTWFP DMKAFWAAEN
ITGTIHNIYT LRGALVRDAL EWSKQINIAL YRFGQDAEVM FASHSWPRWG NDRIQEIMRT
QRDTYAHLNN QVLHLANQGV TINQIHNVYA LPDSLRNQWA AHSYHGSEEH NSRAVVNRYL
GYWDANPATL VPLSPEDSAP LYVEMMGGAK KIIKKGRALY EEGKYLHASE ILNKLVYAEP
KNQTAKDLLA DTFEQIGYQK ESPSVRNSFL AAAYELRHGM PSGASPKASG PDVIRGMSTG
LWLDFLGVRL DTSKTDGKHF IINFVTPDNG EKYLVELSNS ALTNISGVQS SKADLTITMN
RSELNDVMMG KITFDEKIKA GKATLKGNRK PYDELKNMLS TFTMAFELLP GTLPDKKATP
TSGNTFQQAS PADTSGG
//
