ID A0A014KZJ8_9ACTO Unreviewed; 271 AA. AC A0A014KZJ8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 29-OCT-2014, entry version 5. DE RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}; DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}; DE AltName: Full=Lipoate-protein ligase B {ECO:0000256|HAMAP-Rule:MF_00013}; DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|HAMAP-Rule:MF_00013}; DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013}; GN Name=lipB {ECO:0000256|HAMAP-Rule:MF_00013}; GN ORFNames=Z951_41695 {ECO:0000313|EMBL:EXU62426.1}; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1158056 {ECO:0000313|EMBL:EXU62426.1}; RN [1] {ECO:0000313|EMBL:EXU62426.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRh5 {ECO:0000313|EMBL:EXU62426.1}; 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 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262, CC ECO:0000256|SAAS:SAAS00135017}. CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. CC {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262, CC ECO:0000256|SAAS:SAAS00135008}. CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00013, CC ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS00135009}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, CC ECO:0000256|SAAS:SAAS00135012}. 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. {ECO:0000256|HAMAP-Rule:MF_00013}. CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|HAMAP- CC Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXU62426.1}. 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 {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|PIRNR:PIRNR016262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|SAAS:SAAS00135021}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|PIRNR:PIRNR016262}. FT REGION 84 91 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT REGION 195 197 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT REGION 208 210 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT ACT_SITE 226 226 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00013}. FT SITE 192 192 Lowers pKa of active site Cys. FT {ECO:0000256|HAMAP-Rule:MF_00013}. 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 //