ID R6VDL1_9FIRM Unreviewed; 961 AA.
AC R6VDL1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BN546_01828 {ECO:0000313|EMBL:CDC92414.1};
OS Firmicutes bacterium CAG:227.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263010 {ECO:0000313|EMBL:CDC92414.1, ECO:0000313|Proteomes:UP000018294};
RN [1] {ECO:0000313|EMBL:CDC92414.1, ECO:0000313|Proteomes:UP000018294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:227 {ECO:0000313|Proteomes:UP000018294};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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|RuleBase:RU361140};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:CDC92414.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBGC010000133; CDC92414.1; -; Genomic_DNA.
DR AlphaFoldDB; R6VDL1; -.
DR STRING; 1263010.BN546_01828; -.
DR Proteomes; UP000018294; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018294};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..333
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 621..934
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 680
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 683
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 961 AA; 106691 MW; EACBC4F75FB279BD CRC64;
MVKKIKKILS KLCIKRTTVL FIVFAVMFFI LLQRLFVLQI IKGEEYATNF NLTTTKTRTI
KSTRGNIRDR NGELLAHNQL AYSVIIEDNG TYDSTREKNL TLNHVAYEIL KILEENGESV
DVTFHITLDE NGEYAFDTTD FTLDRFKADV YGQAKIEDLS KEEAKASAAR MIEDLSQADR
YGLVNKKKPY TEEERKEYGL PESFTKEEAL DIIKIRYALA ANSFQKYMPA TIATNVSETT
MVAIMEEKDQ LQGVDIQEDS IRVYEDSETF APVIGYTGKA SSEELDELKK ENSNYSSDAV
IGKTGMEQYM ELQLQGTDGE EKLSVDNLGK VLKIDESSKK DPISGNDVYL TIDKNLQKAA
YQILEQKIAG ILASNIISGK TFDKTGLDSS EIRIPIYDVY NALIENSVID ISHFKEEDAS
ETEKAIYSVF SQKQSEVFDS VKAELTVSNP EAFDKLPQEM QDYQSYIVND FLINKKGILS
LDAIDASDAT YIAWSKDHSI SLKEFLTYAA SQNWIDISQF YAEEEYLDSS EVYDALSDYL
TESLTTDSGF SKIIYKYMLQ SDLISGTQLC LVLYDQGVLE ADEATYSALQ AGQKSSYDFM
LDKINSLEIT PAQLALDPCS GSMVVTNVKT GEILACVTYP GYDNNRLANQ MDTDYYSKLS
SDLSRPFYNK ATQQKTAPGS TFKLVTALAG MEEGIATSDY YVNCTGAFTR ISPAINCWYH
AGHGTLGVQG AIKNSCNVFF NQLTYDMGKD KNGEFSDSIG LSKLQKYAKM FQLDKESGIE
LPEAEPEVTD EAAIASSIGQ GTNNYTTSQL ARYATTIASR GTSYSISLLD KVTDSQGNLV
KDYTPEIINQ MDVSDSEWDI IHNGMREVVE NNAAFDDLDY AVSGKTGTAE NTGHPSHGLF
IGFTPSDDPE IAMAVRIANG YSSTNAAAVA KDVIKYEYNL ADESQLLSGT ATSGESTAQT
D
//
