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Database: UniProt
Entry: A0A160NWP2_STRLU
LinkDB: A0A160NWP2_STRLU
Original site: A0A160NWP2_STRLU 
ID   A0A160NWP2_STRLU        Unreviewed;       303 AA.
AC   A0A160NWP2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000256|ARBA:ARBA00017223};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE   AltName: Full=B2 metallo-beta-lactamase {ECO:0000256|ARBA:ARBA00030107};
DE   AltName: Full=Metallo-beta-lactamase type II {ECO:0000256|ARBA:ARBA00033087};
GN   ORFNames=SLA_1229 {ECO:0000313|EMBL:BAU82171.1};
OS   Streptomyces laurentii.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU82171.1, ECO:0000313|Proteomes:UP000217676};
RN   [1] {ECO:0000313|EMBL:BAU82171.1, ECO:0000313|Proteomes:UP000217676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU82171.1,
RC   ECO:0000313|Proteomes:UP000217676};
RA   Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT   "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT   ATCC 31255.";
RL   Genome Announc. 4:e00360-16(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00001526};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC       beta-lactamase family. {ECO:0000256|ARBA:ARBA00005250}.
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DR   EMBL; AP017424; BAU82171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160NWP2; -.
DR   KEGG; slau:SLA_1229; -.
DR   Proteomes; UP000217676; Chromosome.
DR   CDD; cd16282; metallo-hydrolase-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR42951:SF20; BETA LACTAMASE; 1.
DR   PANTHER; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217676};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          27..207
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   303 AA;  33089 MW;  FB1C4C791CE263E9 CRC64;
     MSATDPYVVT LAPHVHAFIQ PDGGWCLNNA GFLGDGGETL LVDTAATERR ALLLRDAVRD
     AGLALPRTIV TTHHHGDHTY GNRVFLPEAR IIGHESCRSE QLAAGRQLHL LWPETDFGHV
     EIEPPHLTYS DRLTLYVGDT EVRVIHPGRA HTIGDSIVHL PRHGIVFTGD LVFNGGTPFV
     LMGSLAGSLR AFDLLRSLDA ETVVPGHGRI TDPSAYAPAE RYLRWVRELA EEGRAKGDTP
     LETARRADLG EFADWPESER LVANLHRAYA ELEGLPEGHP LDLATVFADL TVMNGGRPVA
     CHA
//
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