ID A0A014KZJ8_9ACTO Unreviewed; 271 AA. AC A0A014KZJ8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 09-JUL-2014, entry version 2. DE RecName: Full=Octanoyltransferase; DE EC=2.3.1.181; DE AltName: Full=Lipoate-protein ligase B; DE AltName: Full=Lipoyl/octanoyl transferase; DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase; GN Name=lipB; ORFNames=Z951_41695; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1158056; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRh5; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of RT Streptomyces sp. PRh5, a strain for production of geldanamycin, RT nigericin and nocardamine."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate CC although octanoyl-ACP is likely to be the physiological substrate CC (By similarity). CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of CC octanoic acid is attached via an amide linkage to the epsilon- CC amino group of a specific lysine residue of lipoyl domains of CC lipoate-dependent enzymes (By similarity). CC -!- SIMILARITY: Belongs to the LipB family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JABQ01000105; EXU62426.1; -; Genomic_DNA. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Transferase. FT ACT_SITE 226 226 Acyl-thioester intermediate (By FT similarity){EA10}. FT SITE 192 192 Lowers pKa of active site Cys (By FT similarity). SQ SEQUENCE 271 AA; 29676 MW; F70BDEF4BA58F157 CRC64; MTTSSPGSAP GSPALAYVHL GFGADAVDYE EAWQEQRRVH AARFADEIPD TCLLLEHPPV YTAGRRTADS ERPLDGTPVV DVDRGGKITW HGPGQLVGYP ILKLPRPVDV IAHVRRLEEA LLRTCAEFGL ETTRVEGRSG VWVLGDPVDQ RPALGGLKLD FDPRLEDEEF DARLNGPEYA PSNAGQRRED RKLAAIGVRI AKGVTMHGFS LNCNPDNTWF DRIVPCGIRD AGVTSLSEEL GRDVPISEVL PVVERHLREV LEASVPLPRA V //