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Database: UniProt
Entry: A0A2V5L5K7_9MICC
LinkDB: A0A2V5L5K7_9MICC
Original site: A0A2V5L5K7_9MICC 
ID   A0A2V5L5K7_9MICC        Unreviewed;       652 AA.
AC   A0A2V5L5K7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN   ORFNames=CVV68_20060 {ECO:0000313|EMBL:PYI65003.1};
OS   Arthrobacter livingstonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI65003.1, ECO:0000313|Proteomes:UP000247832};
RN   [1] {ECO:0000313|EMBL:PYI65003.1, ECO:0000313|Proteomes:UP000247832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LI2 {ECO:0000313|EMBL:PYI65003.1,
RC   ECO:0000313|Proteomes:UP000247832};
RA   Liu Q., Xin Y.-H.;
RT   "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT   and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT   glacialis sp. nov.";
RL   Submitted (MAY-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-D beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:PYI65003.1}.
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DR   EMBL; QJVD01000033; PYI65003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5L5K7; -.
DR   OrthoDB; 5241017at2; -.
DR   Proteomes; UP000247832; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR007887; MecA_N.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PROSITE; PS00337; BETA_LACTAMASE_D; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..652
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016005110"
FT   DOMAIN          55..135
FT                   /note="NTF2-like N-terminal transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF05223"
FT   DOMAIN          144..302
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          370..643
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          301..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  65984 MW;  30646BEAF7578A7C CRC64;
     MLRRAAGLLL VLALVLTGAA CSSPKDDGTA TAKSLAAALS AHTVGSVAFD QPAAEVQKEL
     TELSAGIDPL WPKVSVDGVA VKEDGTARIS LGYSWTIPKV EKPWTYKTGA DMKRNGDGWT
     ITWSPAMVEP RLAAGERLKI STAYAARAGI LAADGQAIVK DRPVETVGIN KDGLSEAEGQ
     ASAKALAAVV DIDPAAYLAK IKAYGPVAFV DAITLREEAF AALDQTRLKD IKGFLATPGT
     LPLAPSRTFA QAVLGSVHEA TAEDIKKSKG KIVAGQVVGG SGLQAAFDDQ LAGTPGVTIT
     ATPSATATPS AGATEAPAPA PTPDPNAGGG GAKVLFTQAP TDGKDVKTTL VPKLQTAAED
     ALADVKTPSS IVVMKPSTGA ILAAANGPDS NGYNTAFLGE YAPGSTFKIA TSLGLFREGL
     NPQSTLSCTP EFTADGKKFY NAPGYAVDAE GQIPMTVAIA HSCNTAFVSQ YKNLAQGKLA
     DAAGALGIGM TNDLGLDAFM GAVPRDSAGT EHAASMIGQG KVQVSPLALA TMMSSAVKGA
     TVAPVLVAGH DGKAKPAGDA PLTAKEAEGL RTMMRASVTD GYLTNLADLP GAPAMGKTGT
     AEYGTDNPPR THSWVIAAQG DIAVAVFVED GDLGAITGGP LAKAALEAAV GN
//
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