ID A0A140NM13_PROSM Unreviewed; 380 AA.
AC A0A140NM13;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 OrderedLocusNames=S70_09140 {ECO:0000313|EMBL:AFH93688.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH93688.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH93688.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH93688.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC specificity for cephalosporins. {ECO:0000256|ARBA:ARBA00003808}.
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}.
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DR EMBL; CP003488; AFH93688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140NM13; -.
DR KEGG; psi:S70_09140; -.
DR PATRIC; fig|1157951.4.peg.1826; -.
DR HOGENOM; CLU_020027_10_0_6; -.
DR Proteomes; UP000005012; Chromosome.
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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..380
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007303832"
FT DOMAIN 31..375
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 380 AA; 42960 MW; 65077179A21C406C CRC64;
MKNIFRQRRL FIALSLAMTS ISAFALTQQE VDDIIKPLMK QEQIPGMSVA ISVNGKQAIY
HYGVQSKQTQ IPVSDRTLYE IGSLSKTFTA TLATYAQIQG KLDFSQSVSH YLPELKGSAF
DNVSVMNLAT HTSGLSLFVP SDIKTNDQLM AYYQKWLPDN EVGQYRSYSN LGVGLLGIVT
AKQLNMPFSQ AMEKLMLPSL GLKHTYIHVP KSQEKYYAQG YNKQNQPVRL NLAILGPEAY
GLKSNAKDLI RYLEINMQSI KVAKTWQEAI ENTHTGVYLT DSFVQDMMWE SYPWPVSLSQ
LLQGNRDDMA LKPQKVELIK PAMAPEVRAY YNKTGSSNGF ATYAIFIPEE KIAIVMLSNK
WIPIPQRITA TYQLLEKIER
//
