ID A0A0M4CNK1_SPHS1 Unreviewed; 316 AA.
AC A0A0M4CNK1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=LH20_07160 {ECO:0000313|EMBL:ALC11728.1};
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC11728.1, ECO:0000313|Proteomes:UP000061305};
RN [1] {ECO:0000313|EMBL:ALC11728.1, ECO:0000313|Proteomes:UP000061305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113P3 {ECO:0000313|EMBL:ALC11728.1,
RC ECO:0000313|Proteomes:UP000061305};
RX PubMed=26472829;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT Sphingopyxis sp. 113P3 (NBRC 111507).";
RL Genome Announc. 3:e01169-15(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}.
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DR EMBL; CP009452; ALC11728.1; -; Genomic_DNA.
DR RefSeq; WP_053553587.1; NZ_CP009452.1.
DR AlphaFoldDB; A0A0M4CNK1; -.
DR STRING; 292913.LH20_07160; -.
DR KEGG; sphp:LH20_07160; -.
DR PATRIC; fig|292913.6.peg.1454; -.
DR Proteomes; UP000061305; Chromosome.
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:UP000061305};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..316
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005791475"
FT DOMAIN 63..284
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 316 AA; 33207 MW; A67C65E573BED27D CRC64;
MTIALLSRRR LLSLAPAAGL AGWTMLAGCT PQTSEAPAKP EATPDPIAGR LAALEREAGG
RLGVLFLDSA NGRSAGHRSD ERFALCSTVK WPLAAVVLDA VDAGGLSLDQ RIRFDKSDLL
SNSPRTRENL ARGSMSVAEL LEAAITVSDN AAANLLLPLV GGPEGVTRQF RAWGDAVTRL
DRREPMLNRV GEGEVRDTTT PAAMAALLRT LLLGDALSDA SRKRLIDWGA ATTTGPRRLR
AGLPASWVLA HKTGTAMAPG MMNKYNDIAI AYPPRGAPLL IAAYYEGPVA IEAVRGEDEA
VLAAVGKLAA EWASGA
//
