{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:23:43Z","timestamp":1791307423738,"version":"4.3.1"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[1994,6,1]],"date-time":"1994-06-01T00:00:00Z","timestamp":770428800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1994,6]]},"abstract":"<jats:p>Serratia marcescens S6 produces a pI 9.7 carbapenem-hydrolyzing beta-lactamase that is probably encoded by the chromosome (Y. Yang, P. Wu, and D. M. Livermore, Antimicrob. Agents Chemother. 34:755-758, 1990). A total of 11.3 kb of genomic DNA from this strain was cloned into plasmid pACYC184 in Escherichia coli. After further subclonings, the carbapenem-hydrolyzing beta-lactamase gene (blaSme-1) was sequenced (EMBL accession number Z28968). The gene corresponded to an 882-bp open reading frame which encoded a 294-amino-acid polypeptide. This open reading frame was preceded by a -10 and a -35 region consistent with a putative promoter sequence of members of the family Enterobacteriaceae. This promoter was active in E. coli and S. marcescens, as demonstrated by primer extension analysis. N-terminal sequencing showed that the Sme-1 enzyme had a 27-amino-acid leader peptide and enabled calculation of the molecular mass of the mature protein (29.3 kDa). Sequence alignment revealed that Sme-1 is a class A serine beta-lactamase and not a class B metalloenzyme. The earlier view that the enzyme was zinc dependent was discounted. Among class A beta-lactamases, Sme-1 had the greatest amino acid identity (70%) with the pI 6.9 carbapenem-hydrolyzing beta-lactamase, NMC-A, from Enterobacter cloacae NOR-1. Comparison of these two protein sequences suggested a role for specific residues in carbapenem hydrolysis. The relatedness of Sme-1 to other class A beta-lactamases such as the TEM and SHV types was remote. This work details the sequence of the second carbapenem-hydrolyzing class A beta-lactamase from an enterobacterial species and the first in the genus Serratia.<\/jats:p>","DOI":"10.1128\/aac.38.6.1262","type":"journal-article","created":{"date-parts":[[2012,6,28]],"date-time":"2012-06-28T00:05:50Z","timestamp":1340841950000},"page":"1262-1270","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":159,"title":["Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing class A beta-lactamase, Sme-1, from Serratia marcescens S6"],"prefix":"10.1128","volume":"38","author":[{"given":"T","family":"Naas","sequence":"first","affiliation":[{"name":"Abteilung Mikrobiologie, Universit\u00e4t Basel, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Vandel","sequence":"additional","affiliation":[{"name":"Abteilung Mikrobiologie, Universit\u00e4t Basel, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W","family":"Sougakoff","sequence":"additional","affiliation":[{"name":"Abteilung Mikrobiologie, Universit\u00e4t Basel, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D M","family":"Livermore","sequence":"additional","affiliation":[{"name":"Abteilung Mikrobiologie, Universit\u00e4t Basel, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Nordmann","sequence":"additional","affiliation":[{"name":"Abteilung Mikrobiologie, Universit\u00e4t Basel, Switzerland."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.38.6.1262","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.38.6.1262","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T15:35:33Z","timestamp":1645457733000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.38.6.1262"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,6]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1994,6]]}},"alternative-id":["10.1128\/AAC.38.6.1262"],"URL":"https:\/\/doi.org\/10.1128\/aac.38.6.1262","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,6]]},"assertion":[{"value":"1994-06-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}