MBLFP_SULTO
ID MBLFP_SULTO Reviewed; 261 AA.
AC Q970L2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Metallo-beta-lactamase fold-containing protein ST1585 {ECO:0000303|PubMed:20544975};
DE AltName: Full=Putative quorum sensing signal protein STK_15850 {ECO:0000303|PubMed:20544975};
GN OrderedLocusNames=STK_15850 {ECO:0000312|EMBL:BAB66661.1};
GN ORFNames=ST1585 {ECO:0000312|EMBL:BAB66661.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1] {ECO:0000312|Proteomes:UP000001015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7
RC {ECO:0000312|Proteomes:UP000001015};
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2] {ECO:0007744|PDB:3ADR}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RX PubMed=20544975; DOI=10.1002/prot.22749;
RA Shimada A., Ishikawa H., Nakagawa N., Kuramitsu S., Masui R.;
RT "The first crystal structure of an archaeal metallo-beta-lactamase
RT superfamily protein; ST1585 from Sulfolobus tokodaii.";
RL Proteins 78:2399-2402(2010).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20544975}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000303|PubMed:20544975}.
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DR EMBL; BA000023; BAB66661.1; -; Genomic_DNA.
DR RefSeq; WP_010979639.1; NC_003106.2.
DR PDB; 3ADR; X-ray; 1.80 A; A/B=1-261.
DR PDBsum; 3ADR; -.
DR AlphaFoldDB; Q970L2; -.
DR SMR; Q970L2; -.
DR STRING; 273063.STK_15850; -.
DR EnsemblBacteria; BAB66661; BAB66661; STK_15850.
DR GeneID; 1459625; -.
DR KEGG; sto:STK_15850; -.
DR PATRIC; fig|273063.9.peg.1805; -.
DR eggNOG; arCOG00505; Archaea.
DR OMA; GPRYIAY; -.
DR OrthoDB; 50620at2157; -.
DR BRENDA; 3.5.2.6; 15396.
DR EvolutionaryTrace; Q970L2; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR CDD; cd07726; ST1585-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR037482; ST1585_MBL-fold.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..261
FT /note="Metallo-beta-lactamase fold-containing protein
FT ST1585"
FT /id="PRO_0000433882"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20544975,
FT ECO:0007744|PDB:3ADR"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3ADR"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3ADR"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3ADR"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:3ADR"
FT HELIX 237..259
FT /evidence="ECO:0007829|PDB:3ADR"
SQ SEQUENCE 261 AA; 29182 MW; 1BA2627EB635351D CRC64;
MPCRGLHSIP AGPVEFPEIA TVYVMCGEKL TVMIDAGVSN SIADFSFLDK LDYIVLTHLH
IDHIGLLPEL LQVYKAKVLV KSGFKKYLTS EDGLKKLNES AEKVLGDLYY VYGGLEKKLD
QDKVIEVEGN EEFDLGGYRM RLIYTPGHAR HHMSVLVDDF LFTGDSAGAY FNGVVIPTTP
PVIDYKMYME SLKRQIELKP KVVGFAHGGL VSPKIMEEHL KQMLSKEEIQ INVDIGGVAG
EILRKQIEVN LRGLRESKKS I
