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Database: UniProt
Entry: A0A0W1CI55_9SPHN
LinkDB: A0A0W1CI55_9SPHN
Original site: A0A0W1CI55_9SPHN 
ID   A0A0W1CI55_9SPHN        Unreviewed;       381 AA.
AC   A0A0W1CI55;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=ATE71_18165 {ECO:0000313|EMBL:KTE05502.1};
OS   Sphingopyxis sp. H115.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE05502.1, ECO:0000313|Proteomes:UP000054021};
RN   [1] {ECO:0000313|EMBL:KTE05502.1, ECO:0000313|Proteomes:UP000054021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H115 {ECO:0000313|EMBL:KTE05502.1,
RC   ECO:0000313|Proteomes:UP000054021};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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}.
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:KTE05502.1}.
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DR   EMBL; LNSA01000032; KTE05502.1; -; Genomic_DNA.
DR   RefSeq; WP_058804754.1; NZ_LNSA01000032.1.
DR   AlphaFoldDB; A0A0W1CI55; -.
DR   STRING; 1759073.ATE71_18165; -.
DR   OrthoDB; 9784149at2; -.
DR   Proteomes; UP000054021; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Hydrolase {ECO:0000313|EMBL:KTE05502.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..381
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006920998"
FT   DOMAIN          94..353
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   381 AA;  40278 MW;  E1229445F8E46C5F CRC64;
     MKFEYSGRAL LAVTMSAAVL AGCVSSAAIV PQPRAQQPAA ARGPAGSVTV PIGQPVRSAM
     PAPRGTIDPG FRRAPDGLND RLYSLWRAFP GKTGIAVQRI DGEWTLSQRG DELFPQQSVS
     KLWVALAVLD AVDQGRLRMD QPVRIGPEDL TLFHQPIAAR VRSEGSVTMT VRELIETAIT
     HSDNTANDSL LRTVGGPGAV RAFISKMDLG AIRFGPGERL LQSGTAGLTW QQSYSIGRNF
     QAARSTLAPA TRRAAMDNYL ANPVDGASPA AIASALTRLA RGTLLSPEST DYLLGVMSRT
     RSGPKRLKAG LPAGWKFVHK TGTGQDLNGM TAGYNDIGIA TAPDGTRYAI VVMLGTTTSS
     IPSRMALMQA VSGAVAEFHG K
//
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