ID A0A0L7T6H9_9GAMM Unreviewed; 299 AA.
AC A0A0L7T6H9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=NG42_07070 {ECO:0000313|EMBL:KOC90821.1}, NG43_06145
GN {ECO:0000313|EMBL:KOC94246.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC90821.1, ECO:0000313|Proteomes:UP000037088};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC90821.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC94246.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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:KOC90821.1}.
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DR EMBL; JRXE01000008; KOC90821.1; -; Genomic_DNA.
DR EMBL; JRXF01000007; KOC94246.1; -; Genomic_DNA.
DR RefSeq; WP_052898578.1; NZ_JRXF01000007.1.
DR AlphaFoldDB; A0A0L7T6H9; -.
DR STRING; 1560201.NG42_07070; -.
DR PATRIC; fig|1560201.3.peg.1506; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 InterPro; IPR023650; Beta-lactam_class-A_AS.
DR InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..299
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010427081"
FT DOMAIN 55..270
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 299 AA; 31900 MW; BA6D3064BE253D40 CRC64;
MNSIFSLSRR KYLLAAAGLT IAALFPPSVV LAEQPATLAA QLSALEASAN GRLGVALIDS
GSSRQLSYRG EERFAMASTF KALAAAAVLQ RSVEQPALLN KRIVYQQSEL ITYSPVTEKH
LQQGMTVAEL CAAAVELSDN TAGNILLREI GGPQGITQLA RRLGDNQTRL DRREPALNSA
IPGDVRDTST PLAMAGNLNQ LALGKALPSA QQQLLIQWLK QSKTGAQSIR AGVPQGWQVG
DKTGAGGYGT TNDLAILWPP QGKPLVLAVY FTQHNPQAEA RRDVLASATR LVLAAWEKQ
//
