ID A0A1I6MQN9_9GAMM Unreviewed; 497 AA.
AC A0A1I6MQN9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=SAMN05216570_3668 {ECO:0000313|EMBL:SFS17848.1};
OS Dyella sp. OK004.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFS17848.1, ECO:0000313|Proteomes:UP000198834};
RN [1] {ECO:0000313|EMBL:SFS17848.1, ECO:0000313|Proteomes:UP000198834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK004 {ECO:0000313|EMBL:SFS17848.1,
RC ECO:0000313|Proteomes:UP000198834};
RA de Groot N.N.;
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|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00038473}.
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; FOZI01000004; SFS17848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6MQN9; -.
DR STRING; 1855292.SAMN05216570_3668; -.
DR OrthoDB; 119951at2; -.
DR Proteomes; UP000198834; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017001; P: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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22935:SF95; BETA-LACTAMASE-LIKE 1-RELATED; 1.
DR PANTHER; PTHR22935; PENICILLIN-BINDING PROTEIN; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000198834};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..497
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011499492"
FT DOMAIN 44..363
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT REPEAT 446..479
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 53771 MW; 59937418B703001A CRC64;
MRRSLASVVV GAACLLTVSG LIARDVVPVP DELDRMVQKE GEAFIKAGGA DGLSIAVVRD
GKARFFNFGT KVHGKAQPPD KNTVYEIGSI SKTFTSLLLA HALIEKKAAA SDDMRRYLPG
SYPNLEYQGT PVTLQNLAAT TSALPDNLPD LNAVFKNADP KKALPIAAGM LERYSNQAFF
EDLHKASLID KPGTAPRHSN VAAALLGNIV EKIYGKPYDD LLAQYIEKPL GMQSGVSKAR
LSQAPTGYTG DGSVAPAFNA PYLRAAGGLR YSSADMARYI TAQLDATDLA IKLTQQPVWG
DVDSQAIGFN WVLAKTVDSQ RHLSHSGGTF GFASFMDLYP DAHYGIVFLV NRSGPMTQGQ
LQTMSERIQQ DVFGEPAAVT ALGQALKQGG YKDVDATVKH VRQTHPELHL SEAYVNAWGY
RLLQGGRAND AVGVLEYNTV HYPKSWNAYD SFAEGLEATG DIKRSIANYR RSLELNPENA
HGKERLAKLE KPGESGK
//
