ID   Q6GVZ7_9NEIS            Unreviewed;       389 AA.
AC   Q6GVZ7;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 54.
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:AAT46341.1};
OS   Laribacter hongkongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=168471 {ECO:0000313|EMBL:AAT46341.1};
RN   [1] {ECO:0000313|EMBL:AAT46341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BlaCLHK-2 {ECO:0000313|EMBL:AAT46341.1};
RX   PubMed=15855519; DOI=10.1128/AAC.49.5.1957-1964.2005;
RA   Lau S.K., Ho P.L., Li M.W., Tsoi H.W., Yung R.W., Woo P.C., Yuen K.Y.;
RT   "Cloning and characterization of a chromosomal class C beta-lactamase and
RT   its regulatory gene in Laribacter hongkongensis.";
RL   Antimicrob. Agents Chemother. 49:1957-1964(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY632071; AAT46341.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GVZ7; -.
DR   MEROPS; S12.006; -.
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..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..389
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004273649"
FT   DOMAIN          41..385
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   389 AA;  41589 MW;  925D2EBD1372EF88 CRC64;
     MKKRITPFSR FASKGLFACS AGMLLVTVAH AANTAAAPAG VDAMVQTVMQ AHQIPGMAIA
     IIQPGKTSYH NYGVASRETG QPVRETTLFE IGSLSKPFTA LVAQRAETEG RIDLSAPASR
     YVAALRGSAF DRITLRQLGT YSAGGLPLQF PDNVTTPADM LAYYQHWQPV HPAGTTRLYS
     NPSIGLMGLA ASQATGESFA GLLGTTVLQP LGMNSTYLQV PPEARSRYAM GYTAAGKPVR
     VSPGPLDEET YGIKSTTADM AGFLLAHMDP ARSKDALRSA LQQRAPVYCA GQTRQGLGWE
     SYQDWKNLDV LLAGNSNQMV FEPQPVKACP AGTMNEPDVW VNKTGSTAGF GAYAVFLPAR
     QTGIVILANR NYPITDRIRL AHGILTALH
//