ID   Q6GVZ6_9NEIS            Unreviewed;       390 AA.
AC   Q6GVZ6;
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:AAT46342.1};
OS   Laribacter hongkongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=168471 {ECO:0000313|EMBL:AAT46342.1};
RN   [1] {ECO:0000313|EMBL:AAT46342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BlaCLHK-3 {ECO:0000313|EMBL:AAT46342.1};
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}.
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DR   EMBL; AY632072; AAT46342.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GVZ6; -.
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..390
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004274468"
FT   DOMAIN          42..386
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   390 AA;  41747 MW;  394C26C4E8349EFA CRC64;
     MKKRITPFSR FASKGLFACS AGMLLVTVAH AANMAAAPAG MDAMVQTVMQ AHQIPGMAIA
     IIQPGKTTYH NYGVASRETG QPVRETTLFE IGSLSKPFTA LVAQRAETEG RIDLSAPASR
     YVTALRGSAF DRITLRQLGT YSAGGLPLQF PDNVTTPADV LAYYRHWQPV HPAGSTRLYS
     NPSIGLMGLA ASQATGESFA GLLGTTVLQP LGMNSTYLQV PPEARSRYAM GYTAAGKPVR
     VNPGPLDEET YGVKSTTADM AGFLLAHMDP ARSKGALRSA LQQTRVPVYC AGQTRQGLGW
     ESYQDWKNLD VLLAGNSNQM VFEPQPVKAC LAGTMNEPDV WVNKTGSTAG FGAYAVFLPA
     RQTGIVILAN RNYPIADRIR LAHGILTALH
//