ID A0A1C2H384_9RHOB Unreviewed; 382 AA.
AC A0A1C2H384;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BFP70_18955 {ECO:0000313|EMBL:OCX58204.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX58204.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX58204.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX58204.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-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 class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, 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:OCX58204.1}.
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DR EMBL; MDHA01000089; OCX58204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C2H384; -.
DR STRING; 1889770.BFP70_18955; -.
DR Proteomes; UP000094269; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000094269}.
FT DOMAIN 33..370
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 382 AA; 41145 MW; A963944200EBBE33 CRC64;
MAGLLFGLFA ATTELVAQPL TDTQIADLAR DSFAPVIAEY DIPGLVVGIT LHGQSYFYAT
GVAVRDGRVP ASPDTIFELG SISKIFTATL AALVDSTGGI DLNAPVSTRV PALKGSVFDS
IRLVDLATHV TGGLPLQVPV DVHDVPELVE WMADWTQPRP GMRSYSNVSI GLLGHITAQA
MGLPYAQAVQ DVLFPAMGLR STFVNVPVPA MDRYAYGYDR KTDAPIRVNP GVLADEAYGV
KSTARDMVRL LDLELGQKQA APDLMAALER TREGRAQTAY YTQDMIWEQY PWPVDLAVME
AGNGYDFILS PQPAAKIAPP LPVQDNVILN KTGATNGFGG YVALIPAEDL GIVVLANRNY
PNEARIRATY SLIQSLLTAQ KR
//
