ID   A0A1H0WG77_9PSEU        Unreviewed;       334 AA.
AC   A0A1H0WG77;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE   AltName: Full=Penicillinase {ECO:0000256|ARBA:ARBA00030171};
GN   ORFNames=SAMN05192558_12120 {ECO:0000313|EMBL:SDP89598.1};
OS   Actinokineospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=504798 {ECO:0000313|EMBL:SDP89598.1, ECO:0000313|Proteomes:UP000199651};
RN   [1] {ECO:0000313|Proteomes:UP000199651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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|ARBA:ARBA00001526};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009}.
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DR   EMBL; FNJB01000021; SDP89598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0WG77; -.
DR   STRING; 504798.SAMN05421871_101600; -.
DR   OrthoDB; 4515847at2; -.
DR   Proteomes; UP000199651; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199651};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..334
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011770655"
FT   DOMAIN          72..271
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   REGION          314..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  34791 MW;  0CB96854275A1D83 CRC64;
     MNVTRRSALG LGAVVGATAL GVGATTQASA STPATAAQAC SKIKSAYDRE TTKAAGTWAS
     FITVTGEAAP AVAARADEVV EAYSVNKIAV ATAVLDKVDR GLLTLDQRVD VTADIVSHDG
     DGIFGYDGAY PSSVTLGHVL ANLLTVSDNT AVRLCGLVVP AAELNEILRA KGFVHTQVKP
     VANPNRFYLG KTTARETHTM LQRLVDGTLL SATSSAHMLK VLRSLTSFTD GIRLNMSSAE
     RVRVATKAGW FADGRNEAGI VFDTAGKAAI TFALFASGQF AGDATANKDN YSATHPALRA
     RQVIGRTLLD SVPPVSTPSA RTFSVPQYHP SNGG
//