ID D3NZG0_AZOS1 Unreviewed; 301 AA.
AC D3NZG0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=penP {ECO:0000313|EMBL:BAI73789.1};
GN Synonyms=ampC {ECO:0000313|EMBL:BAI73789.1};
GN OrderedLocusNames=AZL_a02580 {ECO:0000313|EMBL:BAI73789.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510a {ECO:0000313|EMBL:BAI73789.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI73789.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI73789.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI73789.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510a {ECO:0000313|EMBL:BAI73789.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; AP010947; BAI73789.1; -; Genomic_DNA.
DR RefSeq; WP_012975685.1; NC_013855.1.
DR AlphaFoldDB; D3NZG0; -.
DR MEROPS; S11.A01; -.
DR KEGG; azl:AZL_a02580; -.
DR HOGENOM; CLU_031960_6_0_5; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000002040; Plasmid pAB510a.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam 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; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Plasmid {ECO:0000313|EMBL:BAI73789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..301
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003048847"
FT DOMAIN 57..271
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 301 AA; 31763 MW; 844860D6A72C9940 CRC64;
MIGRRGFLVA TGGVLLWSAA AAQAEESKPV KDGKPSGDDG LAAGMAALEE RSGGRLGVAV
LDTATGRLRG WRGDERFPMC STFKFLLAAA VLKSVDQGKD RLDRRIPVTK ADLLPYAPFS
ETRLTGTPPT LAELCEAAVT LSDNTAANLL LPGVGDPAGL TAFLRGIGDQ TTRLDRNEPT
LNSAIPGDPR DTTTPAAMVR GMERLLIGDV LRLDSRWRLV DWLIANKTGD KRLRAGLPAG
WRVGDKTGTG ANGTANDIAI VWPDGRAPVL IASYLTQTAK GFKAQDSIHA EVARTVAGLI
G
//
