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Database: UniProt
Entry: A0A1N6MY37_9GAMM
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Original site: A0A1N6MY37_9GAMM 
ID   A0A1N6MY37_9GAMM        Unreviewed;       295 AA.
AC   A0A1N6MY37;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=XIS1_460071 {ECO:0000313|EMBL:SIP73756.1};
OS   Xenorhabdus innexi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP73756.1, ECO:0000313|Proteomes:UP000196435};
RN   [1] {ECO:0000313|Proteomes:UP000196435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC   Collection) {ECO:0000313|Proteomes:UP000196435};
RA   Gaudriault S.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FTLG01000188; SIP73756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N6MY37; -.
DR   OrthoDB; 9784149at2; -.
DR   Proteomes; UP000196435; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Hydrolase {ECO:0000313|EMBL:SIP73756.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196435};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..295
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012545969"
FT   DOMAIN          52..267
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   295 AA;  32501 MW;  841FB7F0FB083254 CRC64;
     MPKFIHSTVT FLPLLTTLIA FPSQASASDI QQEQMVHQLT ALEKSANGHL GVALINTADH
     SIIGYRANER FPLCSTSKLM AVSALLKKSE TDEKLLNQRV HYKQADLVEY SPITEKHIED
     GMTLTELSAA TLQYSDNTAM NLLLNQLDGP ESVTTFARTL GDNIFRLDRK EPELNLVQPG
     DKRDTSSPQA MAESLYKLAL GDALATNQRA QLVEWLQGNT TGNASIRAGL PKNWVVGDKT
     GRCDYGSTND IAVIWPTENR APFVLVTYFT QPGDKNAKAR PDILAEATRI MIQAE
//
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