ID   LIPB_RHOPS              Reviewed;         255 AA.
AC   Q135D0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN   Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; OrderedLocusNames=RPD_3083;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC       dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC       octanoyl-ACP is likely to be the physiological substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00013};
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:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC       acid is attached via an amide linkage to the epsilon-amino group of a
CC       specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC       {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00013}.
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DR   EMBL; CP000283; ABE40309.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q135D0; -.
DR   SMR; Q135D0; -.
DR   STRING; 316057.RPD_3083; -.
DR   EnsemblBacteria; ABE40309; ABE40309; RPD_3083.
DR   KEGG; rpd:RPD_3083; -.
DR   eggNOG; COG0321; Bacteria.
DR   HOGENOM; CLU_035168_3_0_5; -.
DR   OMA; GEVTYHC; -.
DR   OrthoDB; 1806796at2; -.
DR   BioCyc; RPAL316057:RPD_RS15485-MON; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   CDD; cd16444; LipB; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00013; LipB; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..255
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_1000001120"
FT   DOMAIN          54..238
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        198
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         92..99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         167..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         180..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   SITE            164
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ   SEQUENCE   255 AA;  27371 MW;  7657D49CE57F85B5 CRC64;
     MINFPQHPRQ TLELAGFLPE ASGRAVEWLI SDSQVPYSEA VAAMDSRAAA IAAGDANELV
     WLLEHPPLYT SGTSGQAADL LDPRFPLHAT GRGGQLTYHG PGQRVAYVML DLKRRRPDVR
     AYVAALEQWI IATLEAFNVR GERREDRVGV WVARPDKGVG HEDKIAAIGV RLKRWVSLHG
     IAINVEPDLG HFAAIVPCGI SDPRYGVTSL VDLGLPVTMT DVDLALRASF TTIFGATVNA
     SGSEPAAGSV NSSSV