ID   A0A1H8HM06_9BURK        Unreviewed;       390 AA.
AC   A0A1H8HM06;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=SAMN05428959_102418 {ECO:0000313|EMBL:SEN56658.1};
OS   Duganella sp. CF517.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN56658.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FODC01000002; SEN56658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8HM06; -.
DR   STRING; 1881038.SAMN05428959_102418; -.
DR   Proteomes; UP000198691; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000198691};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..390
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011726293"
FT   DOMAIN          37..381
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   390 AA;  41682 MW;  C18812C7AE31EC5F CRC64;
     MPLPSTLRAA YIAAALYACL LAPSHAAGES AKLRAIIDQA IRPVVAEYDL PGVAVAVTID
     GEASFFNYGL ASREQHVPVT ENTLFELGSI SKTFTATLAS YAVATGRLSL GAHPGKYLPA
     LNGAPIDKAT VLHLGTYTAG GLPLQFPDEV PDGGMVAYFQ QWKPDAEPGT QRRYSNPSLG
     LFGHVAALAM GGNFGDVMER RILPGLGLKH TYIRVPASAM ADYAWGYDKA NQPGRFNPDL
     LSDEAYGIRS SAADMVRYLQ ANIDPSRLET TLRRAVEGTH VGYFEIEGMV QGLGWEQYPY
     PVSLADLQAG NSQTMISQAN PTRPLAPPRT PTQATLFNKT GSTSRFGAYA AFVPAKKIGV
     VILANKNYPI AARVQAARAI LINLEARGAD
//