ID A0A0M0G6E8_SPOGL Unreviewed; 310 AA.
AC A0A0M0G6E8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AF332_00150 {ECO:0000313|EMBL:KON85440.1};
OS Sporosarcina globispora (Bacillus globisporus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1459 {ECO:0000313|EMBL:KON85440.1, ECO:0000313|Proteomes:UP000037109};
RN [1] {ECO:0000313|Proteomes:UP000037109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10036 dsm4.";
RL Submitted (JUL-2015) 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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, 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:KON85440.1}.
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DR EMBL; LGUF01000007; KON85440.1; -; Genomic_DNA.
DR RefSeq; WP_053432827.1; NZ_LGUF01000007.1.
DR AlphaFoldDB; A0A0M0G6E8; -.
DR STRING; 1459.AF332_00150; -.
DR PATRIC; fig|1459.3.peg.47; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000037109; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..310
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005599247"
FT DOMAIN 69..283
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 310 AA; 34023 MW; EFB835D816E12ADE CRC64;
MKKLYYSISG KHTLKAVRLI SMALLLILAG CANANKASEP NMDEASKKTS VNTDQKFKQL
ERDFDARLGV YAYDTGSKKT IAYRSNERFA YASTFKPLAA AILLEKKSLE EMDEIITYKS
DDLVTYSPVT EKHVKTGMTL RELCEAAIRF SDNTAGNLML EELGGPEGFE TALKEMGDSV
TKPSRFETDL NEAEPGDIRD TSTPKELAAS LQKSLMGDLL PEEKQSILTD WMRGNATGDP
LIRAGVPSGW EVADKSGAGG YGTRNDIAIV WPPNREPIIM AILSSRDSKD AEYDNALIAE
AAEMTIKALD
//
