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Beta-lactamase (EC 3.5.2.6) (Ambler class A beta-lactamase)

 BLAC_MYCTU              Reviewed;         307 AA.
P9WKD3; L0T8I9; P0A5I6; P0C5C1; Q10670;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 23.
RecName: Full=Beta-lactamase {ECO:0000303|PubMed:15699201};
EC=3.5.2.6 {ECO:0000269|PubMed:16870770, ECO:0000269|PubMed:17915954, ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175};
AltName: Full=Ambler class A beta-lactamase {ECO:0000303|PubMed:17915954};
Flags: Precursor;
Name=blaC {ECO:0000303|PubMed:15699201}; Synonyms=blaA;
OrderedLocusNames=Rv2068c; ORFNames=MTCY49.07c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
EXPORT VIA THE TAT-SYSTEM, MUTAGENESIS OF 8-ARG-ARG-9, AND SUBCELLULAR
LOCATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16267291; DOI=10.1128/JB.187.22.7667-7679.2005;
McDonough J.A., Hacker K.E., Flores A.R., Pavelka M.S. Jr.,
Braunstein M.;
"The twin-arginine translocation pathway of Mycobacterium smegmatis is
functional and required for the export of mycobacterial beta-
lactamases.";
J. Bacteriol. 187:7667-7679(2005).
[3]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15699201; DOI=10.1099/mic.0.27629-0;
Flores A.R., Parsons L.M., Pavelka M.S. Jr.;
"Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis
and Mycobacterium smegmatis and susceptibility to beta-lactam
antibiotics.";
Microbiology 151:521-532(2005).
[4]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
PubMed=17915954; DOI=10.1021/bi701506h;
Hugonnet J.E., Blanchard J.S.;
"Irreversible inhibition of the Mycobacterium tuberculosis beta-
lactamase by clavulanate.";
Biochemistry 46:11998-12004(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
BIOTECHNOLOGY.
PubMed=23000993; DOI=10.1038/nchem.1435;
Xie H., Mire J., Kong Y., Chang M., Hassounah H.A., Thornton C.N.,
Sacchettini J.C., Cirillo J.D., Rao J.;
"Rapid point-of-care detection of the tuberculosis pathogen using a
BlaC-specific fluorogenic probe.";
Nat. Chem. 4:802-809(2012).
[7]
BIOTECHNOLOGY.
PubMed=24989449; DOI=10.1002/anie.201405243;
Cheng Y., Xie H., Sule P., Hassounah H., Graviss E.A., Kong Y.,
Cirillo J.D., Rao J.;
"Fluorogenic probes with substitutions at the 2 and 7 positions of
cephalosporin are highly BlaC-specific for rapid Mycobacterium
tuberculosis detection.";
Angew. Chem. Int. Ed. Engl. 53:9360-9364(2014).
[8]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 41-307, FUNCTION, CATALYTIC
ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16870770; DOI=10.1128/AAC.00320-06;
Wang F., Cassidy C., Sacchettini J.C.;
"Crystal structure and activity studies of the Mycobacterium
tuberculosis beta-lactamase reveal its critical role in resistance to
beta-lactam antibiotics.";
Antimicrob. Agents Chemother. 50:2762-2771(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 43-307 IN COVALENT COMPLEX
WITH CLAVULANATE INHIBITOR, AND ENZYME REGULATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18422342; DOI=10.1021/bi8001055;
Tremblay L.W., Hugonnet J.E., Blanchard J.S.;
"Structure of the covalent adduct formed between Mycobacterium
tuberculosis beta-lactamase and clavulanate.";
Biochemistry 47:5312-5316(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 43-307 IN COVALENT COMPLEX
WITH MEROPENEM, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19251630; DOI=10.1126/science.1167498;
Hugonnet J.E., Tremblay L.W., Boshoff H.I., Barry C.E.,
Blanchard J.S.;
"Meropenem-clavulanate is effective against extensively drug-resistant
Mycobacterium tuberculosis.";
Science 323:1215-1218(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 43-307 IN COVALENT COMPLEXES
WITH CARBAPENEMS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVE SITE, AND REACTION MECHANISM.
PubMed=20353175; DOI=10.1021/bi100232q;
Tremblay L.W., Fan F., Blanchard J.S.;
"Biochemical and structural characterization of Mycobacterium
tuberculosis beta-lactamase with the carbapenems ertapenem and
doripenem.";
Biochemistry 49:3766-3773(2010).
[12]
X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 43-307 OF MUTANTS ALA-87 AND
ALA-182 IN MICHAELIS COMPLEX AND COVALENT COMPLEX WITH CEFAMANDOLE,
ACTIVE SITE, REACTION MECHANISM, AND MUTAGENESIS OF LYS-87 AND
GLU-182.
PubMed=20961112; DOI=10.1021/bi1015088;
Tremblay L.W., Xu H., Blanchard J.S.;
"Structures of the Michaelis complex (1.2 A) and the covalent acyl
intermediate (2.0 A) of cefamandole bound in the active sites of the
Mycobacterium tuberculosis beta-lactamase K73A and E166A mutants.";
Biochemistry 49:9685-9687(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 43-307 IN COVALENT COMPLEX
WITH NXL104 INHIBITOR, AND ENZYME REGULATION.
PubMed=22587688; DOI=10.1021/bi300508r;
Xu H., Hazra S., Blanchard J.S.;
"NXL104 irreversibly inhibits the beta-lactamase from Mycobacterium
tuberculosis.";
Biochemistry 51:4551-4557(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 43-307 OF MUTANT ALA-236,
ENZYME REGULATION, AND MUTAGENESIS OF SER-142; ARG-236 AND THR-253.
PubMed=24060876; DOI=10.1128/AAC.01253-13;
Kurz S.G., Wolff K.A., Hazra S., Bethel C.R., Hujer A.M., Smith K.M.,
Xu Y., Tremblay L.W., Blanchard J.S., Nguyen L., Bonomo R.A.;
"Can inhibitor-resistant substitutions in the Mycobacterium
tuberculosis beta-Lactamase BlaC lead to clavulanate resistance?: a
biochemical rationale for the use of beta-lactam-beta-lactamase
inhibitor combinations.";
Antimicrob. Agents Chemother. 57:6085-6096(2013).
[15]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 32-307, AND MUTAGENESIS OF
ILE-117.
PubMed=24023821; DOI=10.1371/journal.pone.0073123;
Feiler C., Fisher A.C., Boock J.T., Marrichi M.J., Wright L.,
Schmidpeter P.A., Blankenfeldt W., Pavelka M., DeLisa M.P.;
"Directed evolution of Mycobacterium tuberculosis beta-lactamase
reveals gatekeeper residue that regulates antibiotic resistance and
catalytic efficiency.";
PLoS ONE 8:E73123-E73123(2013).
-!- FUNCTION: Extended spectrum beta-lactamase (ESBL) that inactivates
beta-lactam antibiotics by hydrolyzing the amide group of the
beta-lactam ring. Displays high levels of penicillinase and
cephalosporinase activity as well as measurable activity with
carbapenems, including imipenem and meropenem. Plays a primary
role in the intrinsic resistance of M.tuberculosis to beta-lactam
antibiotics. {ECO:0000269|PubMed:15699201,
ECO:0000269|PubMed:16870770, ECO:0000269|PubMed:17915954,
ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000269|PubMed:16870770,
ECO:0000269|PubMed:17915954, ECO:0000269|PubMed:19251630,
ECO:0000269|PubMed:20353175}.
-!- ENZYME REGULATION: Is inhibited by sulbactam, tazobactam, and
clavulanate. Sulbactam inhibits the enzyme competitively and
reversibly with respect to nitrocefin. Tazobactam inhibits the
enzyme in a time-dependent manner, but the activity of the enzyme
reappears due to the slow hydrolysis of the covalently acylated
enzyme. In contrast, clavulanate reacts with the enzyme quickly to
form hydrolytically stable, inactive forms of the enzyme, via
irreversible acylation of the catalytic serine residue.
Clavulanate has potential to be used in combination with approved
beta-lactam antibiotics to treat multi-drug resistant (MDR) and
extremely drug resistant (XDR) strains of M.tuberculosis. Is also
irreversibly inhibited by NXL104, which forms an extremely stable
carbamoyl adduct with the enzyme but shows an inhibition
efficiency more than 100-fold lower than that of clavulanate. Is
inhibited by carbapenems, that are very poor substrates for the
enzyme. {ECO:0000269|PubMed:17915954, ECO:0000269|PubMed:18422342,
ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:22587688,
ECO:0000269|PubMed:24060876}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 uM for ampicillin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=22 uM for amoxicillin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=19 uM for penicillin G (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=69 uM for penicillin V (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=59 uM for piperacillin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=114 uM for cephalosporin C (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=152 uM for cephalotin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=5100 uM for cefuroxime (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=184 uM for cefamandole (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=127 uM for cefoxitin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=280 uM for ceftazidime (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=520 uM for ceftriaxone (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=5570 uM for cefotaxime (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=57 uM for nitrocefin (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=195 uM for CENTA (at pH 6.4) {ECO:0000269|PubMed:17915954};
KM=9.4 uM for imipenem (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=3.4 uM for meropenem (at pH 6.4)
{ECO:0000269|PubMed:17915954};
KM=63 uM for ampicillin (at pH 7.5)
{ECO:0000269|PubMed:16870770};
KM=117 uM for cephalotin (at pH 7.5)
{ECO:0000269|PubMed:16870770};
KM=195 uM for cefoxitin (at pH 7.5)
{ECO:0000269|PubMed:16870770};
KM=593 uM for ceftazidime (at pH 7.5)
{ECO:0000269|PubMed:16870770};
KM=279 uM for meropenem (at pH 7.5)
{ECO:0000269|PubMed:16870770};
KM=3.4 uM for meropenem (at pH 6.5)
{ECO:0000269|PubMed:19251630};
KM=0.18 uM for doripenem (at pH 6.5)
{ECO:0000269|PubMed:20353175};
KM=0.18 uM for ertapenem (at pH 6.5)
{ECO:0000269|PubMed:20353175};
KM=55 uM for faropenem (at pH 6.5)
{ECO:0000269|PubMed:20353175};
Note=kcat is 600 min(-1) with ampicillin as substrate. kcat is
340 min(-1) with amoxicillin as substrate. kcat is 560 min(-1)
with penicillin G as substrate. kcat is 2100 min(-1) with
penicillin V as substrate. kcat is 690 min(-1) with piperacillin
as substrate. kcat is 1070 min(-1) with cephalosporin C as
substrate. kcat is 490 min(-1) with cephalotin as substrate.
kcat is 490 min(-1) with cefuroxime as substrate. kcat is 3500
min(-1) with cefamandole as substrate. kcat is 48 min(-1) with
cefoxitin as substrate. kcat is 2.0 min(-1) with ceftazidime as
substrate. kcat is 49 min(-1) with ceftriaxone as substrate.
kcat is 380 min(-1) with cefotaxime as substrate. kcat is 6680
min(-1) with nitrocefin as substrate. kcat is 1770 min(-1) with
CENTA as substrate. kcat is 10 min(-1) with imipenem as
substrate. kcat is 0.08 min(-1) with meropenem as substrate.
Assays above performed at pH 6.4. kcat is 18.5 sec(-1) with
ampicillin as substrate. kcat is 12.1 sec(-1) with cephalotin as
substrate. kcat is 1.1 sec(-1) with cefoxitin as substrate. kcat
is 0.2 sec(-1) with ceftazidime as substrate. kcat is 0.9 sec(-
1) with meropenem as substrate. Assays above performed at pH
7.5. kcat is 0.08 min(-1) with meropenem as substrate at pH 6.5.
kcat is 0.016 min(-1) with doripenem as substrate. kcat is 0.017
min(-1) with ertapenem as substrate. kcat is 0.65 min(-1) with
faropenem as substrate. Assays above performed at pH 6.5.
{ECO:0000269|PubMed:16870770, ECO:0000269|PubMed:17915954,
ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17915954}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000303|PubMed:15699201}. Periplasm
{ECO:0000305|PubMed:16267291}. Secreted
{ECO:0000250|UniProtKB:A5U493}.
-!- INDUCTION: Constitutively expressed.
{ECO:0000303|PubMed:24023821}.
-!- PTM: Exported by the Tat system. The position of the signal
peptide cleavage has not been experimentally proven.
{ECO:0000269|PubMed:16267291}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene become significantly
more susceptible (16- to 32-fold) to penicillins as well as third-
generation cephalosporins and carbapenems. They have no detectable
beta-lactamase activity. {ECO:0000269|PubMed:15699201}.
-!- BIOTECHNOLOGY: Can be used as a biomarker, which together with
BlaC-specific fluorogenic substrates, allows a rapid and accurate
detection of very low numbers of M.tuberculosis for the clinical
diagnosis of tuberculosis in sputum and other specimens.
{ECO:0000269|PubMed:23000993, ECO:0000269|PubMed:24989449}.
-!- SIMILARITY: Belongs to the class-A beta-lactamase family.
{ECO:0000305}.
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EMBL; AL123456; CCP44842.1; -; Genomic_DNA.
PIR; G70764; G70764.
RefSeq; NP_216584.1; NC_000962.3.
RefSeq; WP_003410677.1; NZ_KK339370.1.
PDB; 2GDN; X-ray; 1.72 A; A=41-307.
PDB; 3CG5; X-ray; 1.70 A; A=43-307.
PDB; 3DWZ; X-ray; 1.80 A; A=43-307.
PDB; 3IQA; X-ray; 2.20 A; A=43-307.
PDB; 3M6B; X-ray; 1.30 A; A=43-307.
PDB; 3M6H; X-ray; 1.99 A; A=43-307.
PDB; 3N6I; X-ray; 2.00 A; A=43-307.
PDB; 3N7W; X-ray; 1.70 A; A=43-307.
PDB; 3N8L; X-ray; 1.40 A; A=43-307.
PDB; 3N8R; X-ray; 1.41 A; A=43-307.
PDB; 3N8S; X-ray; 2.00 A; A=43-307.
PDB; 3NBL; X-ray; 2.00 A; A=43-307.
PDB; 3NC8; X-ray; 1.50 A; A=43-307.
PDB; 3NCK; X-ray; 2.80 A; A=43-307.
PDB; 3NDE; X-ray; 1.70 A; A=43-307.
PDB; 3NDG; X-ray; 1.90 A; A=43-307.
PDB; 3NY4; X-ray; 1.22 A; A=43-307.
PDB; 3VFF; X-ray; 2.78 A; A/B/C/D=43-307.
PDB; 3VFH; X-ray; 2.57 A; A/B/C/D=43-307.
PDB; 3ZHH; X-ray; 2.85 A; A/B/C/D=32-307.
PDB; 4DF6; X-ray; 2.29 A; A=43-307.
PDB; 4EBL; X-ray; 2.10 A; A/B/C/D=43-307.
PDB; 4EBN; X-ray; 2.85 A; A/B/C/D=43-307.
PDB; 4EBP; X-ray; 2.29 A; A/B/C/D=43-307.
PDB; 4JLF; X-ray; 2.10 A; A=43-307.
PDB; 4Q8I; X-ray; 1.90 A; A=41-307.
PDB; 4QB8; X-ray; 1.76 A; A=42-307.
PDB; 4QHC; X-ray; 1.90 A; A=42-307.
PDB; 4X6T; X-ray; 1.40 A; A=45-307.
PDBsum; 2GDN; -.
PDBsum; 3CG5; -.
PDBsum; 3DWZ; -.
PDBsum; 3IQA; -.
PDBsum; 3M6B; -.
PDBsum; 3M6H; -.
PDBsum; 3N6I; -.
PDBsum; 3N7W; -.
PDBsum; 3N8L; -.
PDBsum; 3N8R; -.
PDBsum; 3N8S; -.
PDBsum; 3NBL; -.
PDBsum; 3NC8; -.
PDBsum; 3NCK; -.
PDBsum; 3NDE; -.
PDBsum; 3NDG; -.
PDBsum; 3NY4; -.
PDBsum; 3VFF; -.
PDBsum; 3VFH; -.
PDBsum; 3ZHH; -.
PDBsum; 4DF6; -.
PDBsum; 4EBL; -.
PDBsum; 4EBN; -.
PDBsum; 4EBP; -.
PDBsum; 4JLF; -.
PDBsum; 4Q8I; -.
PDBsum; 4QB8; -.
PDBsum; 4QHC; -.
PDBsum; 4X6T; -.
ProteinModelPortal; P9WKD3; -.
SMR; P9WKD3; -.
STRING; 83332.Rv2068c; -.
PaxDb; P9WKD3; -.
EnsemblBacteria; CCP44842; CCP44842; Rv2068c.
GeneID; 888742; -.
KEGG; mtu:Rv2068c; -.
TubercuList; Rv2068c; -.
eggNOG; ENOG4108J4B; Bacteria.
eggNOG; COG2367; LUCA.
KO; K17836; -.
OMA; EWMKGNA; -.
PhylomeDB; P9WKD3; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0008800; F:beta-lactamase activity; IDA:MTBBASE.
GO; GO:0033251; F:cephalosporinase activity; IDA:MTBBASE.
GO; GO:0033250; F:penicillinase activity; IDA:MTBBASE.
GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IMP:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IMP:MTBBASE.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR000871; Beta-lactam_class-A.
InterPro; IPR023650; Beta-lactam_class-A_AS.
PRINTS; PR00118; BLACTAMASEA.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00146; BETA_LACTAMASE_A; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Cell inner membrane;
Cell membrane; Complete proteome; Hydrolase; Membrane; Periplasm;
Reference proteome; Secreted; Signal.
SIGNAL 1 34 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 35 307 Beta-lactamase.
/FTId=PRO_0000017005.
REGION 251 253 Substrate binding.
{ECO:0000269|PubMed:19251630,
ECO:0000269|PubMed:20353175,
ECO:0000269|PubMed:20961112}.
ACT_SITE 84 84 Acyl-ester intermediate.
{ECO:0000269|PubMed:19251630,
ECO:0000269|PubMed:20353175,
ECO:0000269|PubMed:20961112}.
ACT_SITE 182 182 Proton acceptor.
{ECO:0000303|PubMed:20353175,
ECO:0000303|PubMed:20961112}.
BINDING 142 142 Substrate. {ECO:0000269|PubMed:19251630,
ECO:0000269|PubMed:20353175,
ECO:0000269|PubMed:20961112}.
SITE 87 87 Increases nucleophilicity of active site
Ser. {ECO:0000303|PubMed:20353175,
ECO:0000303|PubMed:20961112}.
SITE 117 117 Functions as a gatekeeper residue that
regulates substrate accessibility to the
enzyme active site.
{ECO:0000303|PubMed:24023821}.
MUTAGEN 8 9 RR->KK: No longer exported via the Tat-
system. Loss of cell resistance to beta-
lactam antibiotics.
{ECO:0000269|PubMed:16267291}.
MUTAGEN 87 87 K->A: 200000-fold decrease in catalytic
efficiency with cefamandole as substrate.
{ECO:0000269|PubMed:20961112}.
MUTAGEN 117 117 I->F: Significant increase in ampicillin
resistance. 2-fold and 3-fold increase in
catalytic efficiency with ampicillin and
nitrocefin as substrate, respectively,
mainly due to an increase in substrate
affinity. {ECO:0000269|PubMed:24023821}.
MUTAGEN 142 142 S->G: Significant reduction of catalytic
activity for both nitrocefin and
ampicillin. Leads to in vitro clavulanate
resistance and decreased susceptibility
to carbapenem inhibitors, but is still
susceptible to ampicillin-clavulanate in
vivo. {ECO:0000269|PubMed:24060876}.
MUTAGEN 182 182 E->A: Loss of catalytic activity with
cefamandole as substrate.
{ECO:0000269|PubMed:20961112}.
MUTAGEN 236 236 R->A,S: Significant reduction of
catalytic activity for both nitrocefin
and ampicillin. Leads to in vitro
clavulanate resistance and decreased
susceptibility to carbapenem inhibitors,
but is still susceptible to ampicillin-
clavulanate in vivo.
{ECO:0000269|PubMed:24060876}.
MUTAGEN 253 253 T->A: Significant reduction of catalytic
activity for both nitrocefin and
ampicillin. Only minor impairment of the
inactivation by clavulanate. Larger
increase in resistance to carbapenems.
{ECO:0000269|PubMed:24060876}.
MUTAGEN 253 253 T->S: Only minor impairment of catalytic
activity with both nitrocefin and
ampicillin. Still inhibited by
clavulanate and carbapenems.
{ECO:0000269|PubMed:24060876}.
HELIX 44 55 {ECO:0000244|PDB:3NY4}.
STRAND 58 63 {ECO:0000244|PDB:3NY4}.
STRAND 67 69 {ECO:0000244|PDB:3NY4}.
STRAND 72 75 {ECO:0000244|PDB:3NY4}.
HELIX 83 86 {ECO:0000244|PDB:3NY4}.
HELIX 87 97 {ECO:0000244|PDB:3NY4}.
HELIX 100 104 {ECO:0000244|PDB:3NY4}.
HELIX 111 113 {ECO:0000244|PDB:3NY4}.
HELIX 121 123 {ECO:0000244|PDB:3NY4}.
TURN 125 127 {ECO:0000244|PDB:3NY4}.
HELIX 131 140 {ECO:0000244|PDB:3NY4}.
HELIX 144 154 {ECO:0000244|PDB:3NY4}.
HELIX 158 160 {ECO:0000244|PDB:3NY4}.
HELIX 161 170 {ECO:0000244|PDB:3NY4}.
HELIX 184 186 {ECO:0000244|PDB:3NY4}.
STRAND 194 197 {ECO:0000244|PDB:3VFH}.
HELIX 199 210 {ECO:0000244|PDB:3NY4}.
STRAND 212 215 {ECO:0000244|PDB:3NY4}.
HELIX 217 228 {ECO:0000244|PDB:3NY4}.
TURN 234 236 {ECO:0000244|PDB:3NY4}.
HELIX 237 240 {ECO:0000244|PDB:3NY4}.
STRAND 245 254 {ECO:0000244|PDB:3NY4}.
TURN 255 257 {ECO:0000244|PDB:3NY4}.
STRAND 258 266 {ECO:0000244|PDB:3NY4}.
STRAND 272 280 {ECO:0000244|PDB:3NY4}.
HELIX 282 284 {ECO:0000244|PDB:3NY4}.
HELIX 292 306 {ECO:0000244|PDB:3NY4}.
SEQUENCE 307 AA; 32568 MW; 448CB2A0E05F4315 CRC64;
MRNRGFGRRE LLVAMAMLVS VTGCARHASG ARPASTTLPA GADLADRFAE LERRYDARLG
VYVPATGTTA AIEYRADERF AFCSTFKAPL VAAVLHQNPL THLDKLITYT SDDIRSISPV
AQQHVQTGMT IGQLCDAAIR YSDGTAANLL LADLGGPGGG TAAFTGYLRS LGDTVSRLDA
EEPELNRDPP GDERDTTTPH AIALVLQQLV LGNALPPDKR ALLTDWMARN TTGAKRIRAG
FPADWKVIDK TGTGDYGRAN DIAVVWSPTG VPYVVAVMSD RAGGGYDAEP REALLAEAAT
CVAGVLA


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