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Database: UniProt
Entry: A0A0X8GJG9_9BURK
LinkDB: A0A0X8GJG9_9BURK
Original site: A0A0X8GJG9_9BURK 
ID   A0A0X8GJG9_9BURK        Unreviewed;       394 AA.
AC   A0A0X8GJG9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN   Name=ampC {ECO:0000313|EMBL:AMC33325.1};
GN   ORFNames=VN23_01215 {ECO:0000313|EMBL:AMC33325.1};
OS   Janthinobacterium sp. B9-8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC33325.1, ECO:0000313|Proteomes:UP000069577};
RN   [1] {ECO:0000313|EMBL:AMC33325.1, ECO:0000313|Proteomes:UP000069577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-8 {ECO:0000313|EMBL:AMC33325.1,
RC   ECO:0000313|Proteomes:UP000069577};
RA   Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT   "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT   isolated from low temperature sewage.";
RL   Submitted (JAN-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|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR   EMBL; CP014222; AMC33325.1; -; Genomic_DNA.
DR   RefSeq; WP_046351033.1; NZ_CP014222.1.
DR   AlphaFoldDB; A0A0X8GJG9; -.
DR   STRING; 1236179.VN23_01215; -.
DR   KEGG; jab:VN23_01215; -.
DR   OrthoDB; 5377431at2; -.
DR   Proteomes; UP000069577; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017001; P: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; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..394
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007066376"
FT   DOMAIN          41..385
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   394 AA;  42945 MW;  EAEF3F582272461D CRC64;
     MRRKATKLLK ILSVLSCVIS PLSHAAENID QAYIQKIVST AITPIQKQFN IPGMAVAVSI
     DGKNYFYNYG VASKEGKQAV SQDTLFEIGS ISKTFTATLA SYAQINGQLS FSDSVSQHLP
     SLRGSAFDKV SLLNLATHTA GGLPLQVPDE ITNNEQLMDY FKNWQPKHAA GTYRVYSNPS
     IGLLGLITAK SMNTSFEDAI EKKLFPELGM TNSYVNVPAA QMKNYAQGYN KKDAPVRVTP
     GVLASEAYGV KSSSADMIKY INANMQIGKI NDKVQQALIN THSGYFKSGG IIQDLIWEQY
     AYPVELNKLL TGNRDAMAYE ANAASKITPV LAPQSMAWIN KTGSTNGFAA YAAFIPSMKI
     GIVILANKNY PIPPRVMAAY QILSQLDQQT ALKN
//
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