GenomeNet

Database: UniProt
Entry: W1SCH9_9BACI
LinkDB: W1SCH9_9BACI
Original site: W1SCH9_9BACI 
ID   W1SCH9_9BACI            Unreviewed;       257 AA.
AC   W1SCH9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=BAVI_19389 {ECO:0000313|EMBL:ETI67111.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67111.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI67111.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67111.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009}.
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:ETI67111.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ALAN01000105; ETI67111.1; -; Genomic_DNA.
DR   RefSeq; WP_024030046.1; NZ_ALAN01000105.1.
DR   AlphaFoldDB; W1SCH9; -.
DR   STRING; 220686.AA980_03840; -.
DR   PATRIC; fig|1131730.3.peg.4067; -.
DR   eggNOG; COG2367; Bacteria.
DR   OrthoDB; 9775096at2; -.
DR   Proteomes; UP000018877; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT   DOMAIN          27..229
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   257 AA;  28508 MW;  A475BA5ECBEA122C CRC64;
     MLTLEEKLKG EITCFQGRIG IAVEIANKRI SLNSMEVFPS ASVIKVPILI EGLRQAETGK
     INLNELTTID KRVGGSGVLQ ALSAKVSMTI KDLMTLMITV SDNTTTNLLI DLLGMDSINS
     TIEKLSMEHT KLSRKMMDFE AIEQGYNNFT SPSDMIKCLK VINEGDFLSE ESRKLAVEIM
     HYQQFHDKLT AMMDLDLVFA ASKTGGLPNV EHDCAILKYG GKTAYAVVLT DQLDNHFAAK
     HLISKIGKHL YDHLVEE
//
DBGET integrated database retrieval system