Reviewed, UniProtKB/Swiss-Prot Q9S169 (BLA24_ECOLX)

Names and origin

Protein names

Recommended name:
    Beta-lactamase SHV-24
    EC=3.5.2.6

Gene names

Name:	bla
Synonyms:	shv24

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes ampicillin. Can also hydrolyze cephaloridine, aztreonam and ceftazidime with a low catalytic rate. Ref.1
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Sequence similarities	Belongs to the class-A beta-lactamase family.
Biophysicochemical properties	Kinetic parameters: KM=32 µM for ampicillin KM=210 µM for cephaloridine KM=500 µM for aztreonam KM=30 µM for ceftazidime Vmax=0.366 µmol/min/µg enzyme with ampicillin as substrate Vmax=0.434 µmol/min/µg enzyme with cephaloridine as substrate Vmax=0.135 µmol/min/µg enzyme with aztreonam as substrate Vmax=0.008 µmol/min/µg enzyme with ceftazidime as substrate

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	beta-lactam antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-lactamase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 286	265	Beta-lactamase SHV-24		PRO_0000016988
Regions
	Region	230 – 232	3	Substrate binding By similarity
Sites
	Active site	66	1	Acyl-ester intermediate By similarity
	Active site	164	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	73 ↔ 119		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S169-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5EA9990BC8B0AAFF	FASTA	286	31,166
	10 20 30 40 50 60 MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE 70 80 90 100 110 120 RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA 130 140 150 160 170 180 AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARGTTTPA 190 200 210 220 230 240 SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG 250 260 270 280 IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR

References

[1]

"A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the omega-loop." Kurokawa H., Yagi T., Shibata N., Shibayama K., Kamachi K., Arakawa Y. Antimicrob. Agents Chemother. 44:1725-1727(2000) [PubMed: 10817740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: HKY453.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB023477 Genomic DNA. Translation: BAA84973.1.
3D structure databases
HSSP	HSSP built from PDB template 1SHV based on UniProtKB P14557.
SMR	Q9S169. Positions 22-286.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.2.6. 246.
Family and domain databases
InterPro	IPR001466. Beta_lactamase-related. IPR000871. Beta_lactamase_A/D. [Graphical view]
Pfam	PF00144. Beta-lactamase. 1 hit. [Graphical view]
PRINTS	PR00118. BLACTAMASEA.
PROSITE	PS00146. BETA_LACTAMASE_A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BLA24_ECOLX

Accession

Primary (citable) accession number: Q9S169

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)