INCFinder

GenBank ID	CP101380.1
Plasmid name	pSC2016090-mcr-147k
Classification	C1
Length	147 496 bp
GC content	52%
Organism	Salmonella enterica strain SC2016290
Curation	Manually annotated

Plasmid map

Notes

Large parts of the IncC backbone including orf1832 and the site of I1 insertion are missing. The empty site of I2 insertion is intact.

Characteristic genes

Gene name	Length	Location	Length of alignment	Identity (%)	Coverage (%)	E-value
repA	1101	1 - 1101 (+)	1101	100	100	0
RHS1	4254	128129 - 132382 (+)	4254	100	100	0
AriB	1156	30396 - 31549 (+)	1156	100	44	0
AriB	640	22856 - 23495 (+)	640	100	24	0

Antimicrobial resistance genes

Type match	Model name	Model type	Location	E-value	Identity
Strict	floR	protein homolog model	24392 - 25606(+)	0	99.5 %
major facilitator superfamily (MFS) antibiotic efflux pump AMR Gene Family Directed pumping of antibiotic out of a cell to confer resistance. Major facilitator superfamily (MFS) transporters and ABC transporters comprise the two largest and most functionally diverse of the transporter superfamilies. However, MFS transporters are distinct from ABC transporters in both their primary sequence and structure and in the mechanism of energy coupling. As secondary transporters they are, like RND and SMR transporters, energized by the electrochemical proton gradient. chloramphenicol Antibiotic Chloramphenicol is a bacteriostatic antimicrobial originally derived from the bacterium Streptomyces venezuelae. It was the first antibiotic to be manufactured synthetically on a large scale. It functions by inhibiting peptidyl transferase activity of the bacterial ribosome, binding to A2451 and A2452 residues in the 23S rRNA of the 50S ribosomal subunit and preventing peptide bond formation. florfenicol Antibiotic Florfenicol is a fluorine derivative of chloramphenicol, where the nitro group (-NO2) is substituted by a sulfomethyl group (-SO2CH3) and the hydroxyl group (-OH), by a fluorine group (-F). The action mechanism is the same as chloramphenicol's, where the antibiotic binds to the 23S RNA of the 50S subunit of bacterial ribosomes to inhibit protein synthesis. phenicol antibiotic Drug Class Phenicols are broad spectrum bacteriostatic antibiotics acting on bacterial protein synthesis. More specifically, the phenicols block peptide elongation by binding to the peptidyltansferase centre of the 70S ribosome. efflux pump complex or subunit conferring antibiotic resistance Efflux Component Efflux proteins that pump antibiotic out of a cell to confer resistance. antibiotic efflux Resistance Mechanism Antibiotic resistance via the transport of antibiotics out of the cell.
Strict	tet(A)	protein homolog model	26206 - 27405(-)	0	99.75 %
major facilitator superfamily (MFS) antibiotic efflux pump AMR Gene Family Directed pumping of antibiotic out of a cell to confer resistance. Major facilitator superfamily (MFS) transporters and ABC transporters comprise the two largest and most functionally diverse of the transporter superfamilies. However, MFS transporters are distinct from ABC transporters in both their primary sequence and structure and in the mechanism of energy coupling. As secondary transporters they are, like RND and SMR transporters, energized by the electrochemical proton gradient. tetracycline Antibiotic Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome. tetracycline antibiotic Drug Class These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes. efflux pump complex or subunit conferring antibiotic resistance Efflux Component Efflux proteins that pump antibiotic out of a cell to confer resistance. antibiotic efflux Resistance Mechanism Antibiotic resistance via the transport of antibiotics out of the cell.
Strict	catII from Escherichia coli K-12	protein homolog model	62885 - 63526(-)	4.28881e-163	98.12 %
chloramphenicol acetyltransferase (CAT) AMR Gene Family Inactivates chloramphenicol by addition of an acyl group. cat is used to describe many variants of the chloramphenicol acetyltransferase gene in a range of organisms including Acinetobacter calcoaceticus, Agrobacterium tumefaciens, Bacillus clausii, Bacillus subtilis, Campylobacter coli, Enterococcus faecalis, Enterococcus faecium, Lactococcus lactis, Listeria monocytogenes, Listonella anguillarum Morganella morganii, Photobacterium damselae subsp. piscicida, Proteus mirabilis, Salmonella typhi, Serratia marcescens, Shigella flexneri, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus intermedius, Streptococcus agalactiae, Streptococcus suis and Streptomyces acrimycini chloramphenicol Antibiotic Chloramphenicol is a bacteriostatic antimicrobial originally derived from the bacterium Streptomyces venezuelae. It was the first antibiotic to be manufactured synthetically on a large scale. It functions by inhibiting peptidyl transferase activity of the bacterial ribosome, binding to A2451 and A2452 residues in the 23S rRNA of the 50S ribosomal subunit and preventing peptide bond formation. phenicol antibiotic Drug Class Phenicols are broad spectrum bacteriostatic antibiotics acting on bacterial protein synthesis. More specifically, the phenicols block peptide elongation by binding to the peptidyltansferase centre of the 70S ribosome. antibiotic inactivation Resistance Mechanism Enzymatic inactivation of antibiotic to confer drug resistance.
Perfect	CTX-M-55	protein homolog model	64574 - 65449(-)	0	100 %
CTX-M beta-lactamase AMR Gene Family These enzymes were named for their greater activity against cefotaxime than other oxyimino-beta-lactam substrates (eg, ceftazidime, ceftriaxone, or cefepime). Rather than arising by mutation, they represent examples of plasmid acquisition of beta-lactamase genes normally found on the chromosome of Kluyvera species, a group of rarely pathogenic commensal organisms. These enzymes are not very closely related to TEM or SHV beta-lactamases in that they show only approximately 40% identity with these two commonly isolated beta-lactamases. Despite their name, a few are more active on ceftazidime than cefotaxime. CTX-M-15 was recently found in bacterial strains expressing NDM-1 and were responsible for resistance to aztreonam. ceftazidime Antibiotic Ceftazidime is a third-generation cephalosporin antibiotic. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. Unlike most third-generation agents, it is active against Pseudomonas aeruginosa, however it has weaker activity against Gram-positive microorganisms and is not used for such infections. ceftriaxone Antibiotic Ceftriaxone is a third-generation cephalosporin antibiotic. The presence of an aminothiazolyl sidechain increases ceftriazone's resistance to beta-lactamases. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. 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. antibiotic inactivation Resistance Mechanism Enzymatic inactivation of antibiotic to confer drug resistance.
Perfect	TEM-1	protein homolog model	67465 - 68325(+)	0	100 %
TEM beta-lactamase AMR Gene Family TEM-1 is the most commonly-encountered beta-lactamase in gram-negative bacteria. Up to 90% of ampicillin resistance in E. coli is due to the production of TEM-1. Also responsible for the ampicillin and penicillin resistance that is seen in H. influenzae and N. gonorrhoeae in increasing numbers. Although TEM-type beta-lactamases are most often found in E. coli and K. pneumoniae, they are also found in other species of gram-negative bacteria with increasing frequency. The amino acid substitutions responsible for the ESBL phenotype cluster around the active site of the enzyme and change its configuration, allowing access to oxyimino-beta-lactam substrates. Opening the active site to beta-lactam substrates also typically enhances the susceptibility of the enzyme to b-lactamase inhibitors, such as clavulanic acid. Although the inhibitor-resistant beta-lactamases are not ESBLs, they are often discussed with ESBLs because they are also derivatives of the classical TEM- or SHV-type enzymes. These enzymes were at first given the designation IRT for inhibitor-resistant TEM beta-lactamase; however, all have subsequently been renamed with numerical TEM designations. There are at least 19 distinct inhibitor-resistant TEM beta-lactamases. Inhibitor-resistant TEM beta-lactamases have been found mainly in clinical isolates of E. coli, but also some strains of K. pneumoniae, Klebsiella oxytoca, P. mirabilis, and Citrobacter freundii. Although the inhibitor-resistant TEM variants are resistant to inhibition by clavulanic acid and sulbactam, thereby showing clinical resistance to the beta-lactam-lactamase inhibitor combinations of amoxicillin-clavulanate (Co-amoxiclav), ticarcillin-clavulanate, and ampicillin/sulbactam, they normally remain susceptible to inhibition by tazobactam and subsequently the combination of piperacillin/tazobactam, although resistance has been described. amoxicillin Antibiotic Amoxicillin is a moderate-spectrum, bacteriolytic, beta-lactam antibiotic used to treat bacterial infections caused by susceptible microorganisms. A derivative of penicillin, it has a wider range of treatment but remains relatively ineffective against Gram-negative bacteria. It is commonly taken with clavulanic acid, a beta-lactamase inhibitor. Like other beta-lactams, amoxicillin interferes with the synthesis of peptidoglycan. ampicillin Antibiotic Ampicillin is a penicillin derivative that is highly acid stable, with its activity similar to benzylpenicillin. cefalotin Antibiotic Cefalotin is a semisynthetic cephalosporin antibiotic activate against staphylococci. It is resistant to staphylococci beta-lactamases but hydrolyzed by enterobacterial beta-lactamases. 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. 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. penem Drug Class Penems are a class of unsaturated beta-lactam antibiotics with a broad spectrum of antibacterial activity and have a structure which renders them highly resistant to beta-lactamases. All penems are all synthetically made and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. They are structurally similar to carbapenems, however, where carbapenems have a carbon, penems have a sulfur. antibiotic inactivation Resistance Mechanism Enzymatic inactivation of antibiotic to confer drug resistance.