INCFinder

GenBank ID	MZ475694.1
Plasmid name	unnamed2
Classification	C2
Length	99 645 bp
GC content	54%
Organism	Klebsiella pneumoniae strain HS11286-vir2
Curation	Manually annotated

Plasmid map

Notes

Large parts of the IncC backbone including RHS, orf1847/1832 and the site of I2 insertion are missing. The presence of I1 insertion suggests that the plasmid is an IncC2 derivative.

Characteristic genes

Gene name	Length	Location	Length of alignment	Identity (%)	Coverage (%)	E-value
repA	1101	63820 - 64920 (+)	1101	100	100	0
I1	428	84648 - 85075 (+)	428	100	100	0

Antimicrobial resistance genes

Type match	Model name	Model type	Location	E-value	Identity
Perfect	KPC-1	protein homolog model	39761 - 40642(+)	0	100 %
antibiotic inactivation Resistance Mechanism Enzymatic inactivation of antibiotic to confer drug resistance. cephalosporin Drug Class Cephalosporins are a class of beta-lactam antibiotics, containing the beta-lactam ring fused with a dihydrothiazolidine ring. Together with cephamycins they belong to a sub-group called cephems. Cephalosporin are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. penam Drug Class Penams, often referred to as penicillins, are a group of antibiotics derived from Penicillium fungi. Penicillin antibiotics are historically significant because they are the first drugs that were effective against many previously serious diseases such as syphilis and Staphylococcus infections. Penicillins are still widely used today, though many types of bacteria are now resistant. All penicillins are beta-lactam antibiotics in the penam sub-group, and are used in the treatment of bacterial infections caused by susceptible, usually Gram-positive, organisms. monobactam Drug Class Monobactams are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Unlike penams and cephems, monobactams do not have any ring fused to its four-member lactam structure. Monobactam antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. carbapenem Drug Class Carbapenems are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Carbapenem antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. KPC beta-lactamase AMR Gene Family Klebsiella pneumoniae carbapenem resistant (KPC) beta-lactamases are notorious for their ability to efficiently hydrolyze carbapenems, unlike other Ambler Class A beta-lactamases. There are currently 9 variants reported worldwide. These enzymes were first isolated from Klebsiella pneumoniae strains in 2001 in the United States. Hospital outbreaks have since been reported in Greece and Israel and KPC carrying strains are now endemic to New York facilities. KPC-1 and KPC-2 have been shown to be identical and are now referred to as KPC-2.
Perfect	KPC-1	protein homolog model	95497 - 96378(+)	0	100 %
antibiotic inactivation Resistance Mechanism Enzymatic inactivation of antibiotic to confer drug resistance. cephalosporin Drug Class Cephalosporins are a class of beta-lactam antibiotics, containing the beta-lactam ring fused with a dihydrothiazolidine ring. Together with cephamycins they belong to a sub-group called cephems. Cephalosporin are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. penam Drug Class Penams, often referred to as penicillins, are a group of antibiotics derived from Penicillium fungi. Penicillin antibiotics are historically significant because they are the first drugs that were effective against many previously serious diseases such as syphilis and Staphylococcus infections. Penicillins are still widely used today, though many types of bacteria are now resistant. All penicillins are beta-lactam antibiotics in the penam sub-group, and are used in the treatment of bacterial infections caused by susceptible, usually Gram-positive, organisms. monobactam Drug Class Monobactams are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Unlike penams and cephems, monobactams do not have any ring fused to its four-member lactam structure. Monobactam antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. carbapenem Drug Class Carbapenems are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Carbapenem antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. KPC beta-lactamase AMR Gene Family Klebsiella pneumoniae carbapenem resistant (KPC) beta-lactamases are notorious for their ability to efficiently hydrolyze carbapenems, unlike other Ambler Class A beta-lactamases. There are currently 9 variants reported worldwide. These enzymes were first isolated from Klebsiella pneumoniae strains in 2001 in the United States. Hospital outbreaks have since been reported in Greece and Israel and KPC carrying strains are now endemic to New York facilities. KPC-1 and KPC-2 have been shown to be identical and are now referred to as KPC-2.