ID A0A3L6ZWF0_9MICO Unreviewed; 314 AA.
AC A0A3L6ZWF0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=D9V29_04090 {ECO:0000313|EMBL:RLP72343.1};
OS Mycetocola manganoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=699879 {ECO:0000313|EMBL:RLP72343.1, ECO:0000313|Proteomes:UP000270299};
RN [1] {ECO:0000313|EMBL:RLP72343.1, ECO:0000313|Proteomes:UP000270299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB209002 {ECO:0000313|EMBL:RLP72343.1,
RC ECO:0000313|Proteomes:UP000270299};
RA Li J.;
RL Submitted (OCT-2018) 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}.
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:RLP72343.1}.
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; RCUV01000005; RLP72343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6ZWF0; -.
DR OrthoDB; 3171327at2; -.
DR Proteomes; UP000270299; 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; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 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, ECO:0000313|EMBL:RLP72343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270299}.
FT DOMAIN 8..302
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 314 AA; 32783 MW; 55CF7C9D364D3423 CRC64;
MIPNATELER RLGRRHPVVG AAVVAPGGTT LVVRGATTES DFEIGSVSKG ITGLLYTDAV
ERGEVAPTTQ LGDLLPVHGA AGRVTLGALS THTSGLPRLP AAAQPYRRTL QLWRHGTNPY
GESLDELLEQ VRGVTPGTPK PSYSNLGYEL LGHAVARAAG LGYRELVAQR LTSPLGLDSM
YVPSDRSELR STAVIGRSKR GRTMQPWTGE GIAPAGGIRS SIGDMARLAE SLLDGSAPGT
AALDPVQTFS GGVRIGAAWL TLPFKGRDVT WHNGGTGGFR SWMGLDRTAG TAAIILSATS
ASVDRAGFLL LQGA
//