ID I4Z9P6_9BACT Unreviewed; 321 AA.
AC I4Z9P6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=PrebiDRAFT_1215 {ECO:0000313|EMBL:EIM32938.1};
OS Prevotella bivia DSM 20514.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM32938.1, ECO:0000313|Proteomes:UP000002786};
RN [1] {ECO:0000313|EMBL:EIM32938.1, ECO:0000313|Proteomes:UP000002786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM32938.1,
RC ECO:0000313|Proteomes:UP000002786};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; JH660660; EIM32938.1; -; Genomic_DNA.
DR RefSeq; WP_004339683.1; NZ_JH660660.1.
DR AlphaFoldDB; I4Z9P6; -.
DR GeneID; 78531201; -.
DR HOGENOM; CLU_031960_0_1_10; -.
DR Proteomes; UP000002786; 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: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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002786};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..289
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 321 AA; 35377 MW; 6AD3A50316F0BDFA CRC64;
MEKNRKKQIV VLSIALVCIF ILVFSLFHKS ATKDSANPPL TNVLTDSISQ IVSACPGEIG
VAVIVNNRDT VKVNNKSVYP MMSVFKVHQA LALCNDFDNK GISLDTLVNI NRDKLDPKTW
SPMLKDYSGP VISLTVRDLL RYTLTQSDNN ASNLMFKDMV NVAQTDSFIA TLIPRSSFQI
AYTEEEMSAD HNKAYSNYTS PLGAAMLMNR LFTEGLIDDE KQSFIKNTLK ECKTGVDRIA
APLLDKEGVV IAHKTGSGYV NENGVLAAHN DVAYICLPNN ISYTLAVFVK DFKGNESQAS
QYVAHISAVV YSLLMQTSVK S
//
