ID A0A2P8DE92_9ACTN Unreviewed; 709 AA.
AC A0A2P8DE92;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CLV30_12920 {ECO:0000313|EMBL:PSK95551.1};
OS Haloactinopolyspora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Haloactinopolyspora.
OX NCBI_TaxID=648780 {ECO:0000313|EMBL:PSK95551.1, ECO:0000313|Proteomes:UP000243528};
RN [1] {ECO:0000313|EMBL:PSK95551.1, ECO:0000313|Proteomes:UP000243528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45211 {ECO:0000313|EMBL:PSK95551.1,
RC ECO:0000313|Proteomes:UP000243528};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PSK95551.1}.
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DR EMBL; PYGE01000029; PSK95551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8DE92; -.
DR Proteomes; UP000243528; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Cell cycle {ECO:0000313|EMBL:PSK95551.1};
KW Cell division {ECO:0000313|EMBL:PSK95551.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000243528}.
FT DOMAIN 91..169
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 178..334
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 402..705
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 340..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 72119 MW; 18A9D7BECF7772A2 CRC64;
MLGERGGSAT ERPDEWWLSA ARDFDQHDRR SMKDINVWRC AVTALAAVAV AGAAAGCSGP
PDADPVAEQL ASAVASGEFG DVPMADAAGA DVSAAVADLT EGMDGAPRQV EVVEVRDDGD
DRRAVDLELS WDVGGQEPWT YTTTAALVLV DEQWRVEWSP DVVHPELTSG ARLDVDRQQA
ERGDIVGADG QVIVTERPVY RIGVDKTQVE AGEVEATARE LADLVGVDAD GLAERAEAAG
AKAFVEAITF READAAPVLG AVAELDGAIA LDDTLALAPT REFARPILGT VGEATAEIIE
ESDGRLGVGD VVGLSGLQRQ YDARLRGKPG VTVQIVLPDD AAGESGSGSE SGSGSESGAE
SGEPVVVYES EPSAGADLTT TLDVEVQDRA EQILADVDPA SAIVAVRPSD GAVLAAASGP
GGEGYSTATL GQYAPGSTFK IVTSLALLRA GMDPGTTLSC TPTVTVEGKT FENYDDYPAD
AVGDIPLRSA VAHSCNTALI DRHDTVTQRE LADAAGSLGI GAGHDVGGPA FLGDVPVEAG
ATEHAASMIG QGKVLASPLA MATMAASVAA GRTVTPELVA AEDAAGDETD DAAGDEAGEE
PTAAEPSASP SSSSSRAPAA PLAPGEADVL SELMRGVVED GSASFLADVP GDPVGAKTGT
AEYGSESPPR THAWMVAVQG DLAVAVFVED GESGSQTAGP LLEEFLTDD
//
