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LOCUS YP_005224548 151 aa linear CON 02-JUN-2020 [Klebsiella pneumoniae subsp. pneumoniae HS11286]. ACCESSION YP_005224548 VERSION YP_005224548.1 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 151) 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 151) 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 151) 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 AEW58946. RefSeq Category: Reference Genome CLI: Clinical Isolate Method: conceptual translation. FEATURES Location/Qualifiers source 1..151 /organism="Klebsiella pneumoniae subsp. pneumoniae HS11286" /strain="HS11286" /sub_species="pneumoniae" /db_xref="taxon:1125630" Protein 1..151 /product="UDP-3-O-(3-hydroxymyristoyl)-glucosamine N-acyltransferase" /calculated_mol_wt=16210 Region 31..149 /region_name="LbH_WxcM_N_like" /note="WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization...; cd03358" /db_xref="CDD:100048" Site order(52,54,62,70,72,78,84..85,87,104,106,109,127,143) /site_type="other" /note="putative trimer interface [polypeptide binding]" /db_xref="CDD:100048" Site order(54,56,84,87,106,108..109,114,125..126,131..132, 141..142,144) /site_type="active" /note="putative active site [active]" /db_xref="CDD:100048" Site order(54,56,84) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:100048" Site order(84,87,106,108..109,114,123,125..126,131..132,139, 141..142,144,148) /site_type="other" /note="putative CoA binding site [chemical binding]" /db_xref="CDD:100048" CDS 1..151 /locus_tag="KPHS_02480" /coded_by="complement(NC_016845.1:289103..289558)" /transl_table=11 /db_xref="GeneID:11845235" CONTIG join(WP_002884634.1:1..151) ORIGIN 1 mpelrdtgvr nvvcgenvvi yqpanlydcq lgdnvfvgpf veiqrntrig anskiqshtf 61 iceyvtigqr cfighgvmfa ndlfregkpn adraswgrie igddvsigsg atilavsicd 121 gvvigagsvv tksitekgvw agnparllrr l