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Database: UniProt
Entry: A0A3L6ZWF0_9MICO
LinkDB: A0A3L6ZWF0_9MICO
Original site: A0A3L6ZWF0_9MICO 
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}.
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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
//
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