ID   LIPB_PARVE              Reviewed;         155 AA.
AC   Q00520;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
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;
DE   Flags: Fragment;
GN   Name=lipB;
OS   Paracoccus versutus (Thiobacillus versutus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=34007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25364 / DSM 582 / JCM 20754 / NBRC 14567 / VKM B-2163;
RX   PubMed=1339423; DOI=10.1128/jb.174.11.3707-3714.1992;
RA   Ubbink M., van Beeumen J., Canters G.W.;
RT   "Cytochrome c550 from Thiobacillus versutus: cloning, expression in
RT   Escherichia coli, and purification of the heterologous holoprotein.";
RL   J. Bacteriol. 174:3707-3714(1992).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- 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 {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000305}.
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DR   EMBL; X62808; CAA44626.1; -; Genomic_DNA.
DR   PIR; S23629; S23629.
DR   AlphaFoldDB; Q00520; -.
DR   SMR; Q00520; -.
DR   STRING; 34007.IT40_05930; -.
DR   eggNOG; COG0321; Bacteria.
DR   UniPathway; UPA00538; UER00592.
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   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..155
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_0000062857"
FT   DOMAIN          1..154
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        116
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         5..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            82
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   155 AA;  16914 MW;  89DDE828A3B1D930 CRC64;
     HAVGRGGQYT YHGPGQRLVY VMLDLNRRGR DVRAFVKALE SWVIDALAEF NLKGEIRDGR
     VGVWIARPDK ASLPDGSMRE DKIAAIGVKL RRWVSFHGIS INVEPDLGHY AGIVPCGIQG
     HGVTSLVDMG LPVGMGDLDL ALRRSFARNF PPLGG