ID W0HZX8_9GAMM Unreviewed; 284 AA.
AC W0HZX8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=Sant_P0341 {ECO:0000313|EMBL:AHF79376.1};
OS Sodalis praecaptivus.
OG Plasmid pHS1 {ECO:0000313|EMBL:AHF79376.1,
OG ECO:0000313|Proteomes:UP000019028}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF79376.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF79376.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF79376.1,
RC ECO:0000313|Proteomes:UP000019028};
RC PLASMID=Plasmid pHS1 {ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP006570; AHF79376.1; -; Genomic_DNA.
DR RefSeq; WP_040133580.1; NZ_CP006570.1.
DR AlphaFoldDB; W0HZX8; -.
DR KEGG; sod:Sant_P0341; -.
DR PATRIC; fig|1239307.3.peg.4907; -.
DR HOGENOM; CLU_031960_6_0_6; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000019028; Plasmid pHS1.
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 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.
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 Plasmid {ECO:0000313|EMBL:AHF79376.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019028};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..284
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004789942"
FT DOMAIN 44..260
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 284 AA; 31034 MW; ED6AA39E43577428 CRC64;
MRLIPAVIAA FYFWLSPPVQ ALTTAGLQPY LQKEENRLNA RIGVAILDAH GQRIFGYRSE
ERFPLNSTHK VLACAALLAN ARQHSALLEQ HVTIMPQALV DYSPITQTRL APGKFTLREL
CRAAVSYSDN TAANSILEVI GGAGAVTRFM RLIGDNVTRL DRLEPSLNEA VPGDVRDTTT
PASVVAALRT ILATDVLTLP HRQLLQTWMM DDQVAGDLLR ASLPTGWRIA DKTGAGGYGS
RSIIAAVYPD PKQPFYIAIY ITQTAATLQQ SNRVAANIGK IIFR
//
