ID A0A1E7KC88_9ACTN Unreviewed; 348 AA.
AC A0A1E7KC88;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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|RuleBase:RU361140};
GN ORFNames=AN217_23085 {ECO:0000313|EMBL:OEV01520.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV01520.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEV01520.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV01520.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEV01520.1}.
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DR EMBL; LJGV01000022; OEV01520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7KC88; -.
DR PATRIC; fig|943816.4.peg.4170; -.
DR Proteomes; UP000175829; 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:SF7; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 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:UP000175829}.
FT DOMAIN 18..327
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 348 AA; 36463 MW; 5D63789329572645 CRC64;
MNTCGSEAAL TDRLAREVAR VDAPDVVFGV TRHGRRTVVA GGRAQPPATP REALRYELGS
LSKTYTVLLL ATLAEEGVLH QDDPLTAHLP PGVRPVHPAA HRITLRHLAT HTSGLPRVPP
ALVPGALLRP HSNGYARFGT ERLLRSFAAT RPRHPAGRRW IYSNFGIALL GPALSGAGGG
SFPAVLGTRV LRPLGLTGTT LGPGPAGADA VGHRRDGRTP VPAADMGGFG AAGAVRATPH
DLLGFLEAHL SPADTPLSGP LHAVRRPQLH RGGERGETHT LTWFQHPAPG GPLLFHAGAT
FGQQAFCGFH PASGTGLAAV ATRRYRGCRL VPTAYELLYA LVEEAAAG
//
