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
//