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LOCUS YP_005226304 431 aa linear CON 02-JUN-2020 pneumoniae HS11286]. ACCESSION YP_005226304 VERSION YP_005226304.1 DBLINK BioProject: PRJNA84387 Assembly: GCF_000240185.1 DBSOURCE REFSEQ: accession NC_016845.1 KEYWORDS RefSeq. SOURCE Klebsiella pneumoniae subsp. pneumoniae HS11286 ORGANISM Klebsiella pneumoniae subsp. pneumoniae HS11286 Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella; Klebsiella pneumoniae complex. REFERENCE 1 (residues 1 to 431) AUTHORS Liu,P., Li,P., Jiang,X., Bi,D., Xie,Y., Tai,C., Deng,Z., Rajakumar,K. and Ou,H.Y. TITLE Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae HS11286, a multidrug-resistant strain isolated from human sputum JOURNAL J. Bacteriol. 194 (7), 1841-1842 (2012) PUBMED 22408243 REFERENCE 2 (residues 1 to 431) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (06-FEB-2012) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 3 (residues 1 to 431) AUTHORS Ou,H.-Y., Jiang,X., Liu,P. and Li,P. TITLE Direct Submission JOURNAL Submitted (14-DEC-2011) State Key Laboratory of Microbial Metabolism, Shanghai Jiaotong University, 1954 Huashan Road, Shanghai 200030, China COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence is identical to AEW60702. RefSeq Category: Reference Genome CLI: Clinical Isolate Method: conceptual translation. FEATURES Location/Qualifiers source 1..431 /organism="Klebsiella pneumoniae subsp. pneumoniae HS11286" /strain="HS11286" /sub_species="pneumoniae" /db_xref="taxon:1125630" Protein 1..431 /product="crotonobetaine/carnitine-CoA ligase" /calculated_mol_wt=46779 Region 5..420 /region_name="Adenylate forming domain, Class I superfamily" /note="This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate...; cl17068" /db_xref="CDD:473059" Site order(71,74..79,81..82) /site_type="other" /note="acyl-activating enzyme (AAE) consensus motif" /db_xref="CDD:341228" Site order(74,191..192,213..218,306,318,321,332,412) /site_type="other" /note="AMP binding site [chemical binding]" /db_xref="CDD:341228" Site order(74,116..117,164,166..167,170,191..192,213..218,306, 318,321,329..332,393) /site_type="active" /db_xref="CDD:341228" Site order(116,166..167,170,191,329..331,387,393) /site_type="other" /note="CoA binding site [chemical binding]" /db_xref="CDD:341228" CDS 1..431 /locus_tag="KPHS_20040" /coded_by="NC_016845.1:2066473..2067768" /transl_table=11 /db_xref="GeneID:11847022" CONTIG join(WP_014342997.1:1..431) ORIGIN 1 mkccffdqtf lplvaqllpq lptvkhvvlm esrseaalsq lpsllfyddl lqqgmadyrw 61 pqlneltpas lcytsgttgr pkgvlnthrs lvlhalsgnq pdaagisakd sllpvvpmfh 121 vnawgtpfia amvgarlvlp gphldgdsll qllaaekvtv gfgvpviwag llaamrrtev 181 rlpefkralv ggsalppsma eafqrdygia lthawgmtet spigtintpl skhdalpaqe 241 qqkqcagqgr pifgielqvv dvdgeplprd gqsqgylqvr ghwvveqyyg qdasaltaag 301 wfdtgdigtl dangylvisd rakdiiksgg ewistvelen iaiahpgvrs aaaiaarhpr 361 wderpvllcv raeggeveet dllswfekrv pkwqipdrvi fvdalpvsat gkvlknqlrq 421 aygeilmseg k