ID   LIPB_CYACA              Reviewed;         214 AA.
AC   O19898;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable 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;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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: Plastid, chloroplast.
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; AF022186; AAB82691.1; -; Genomic_DNA.
DR   PIR; T11966; T11966.
DR   RefSeq; NP_045070.1; NC_001840.1.
DR   AlphaFoldDB; O19898; -.
DR   SMR; O19898; -.
DR   PRIDE; O19898; -.
DR   GeneID; 800233; -.
DR   UniPathway; UPA00538; UER00592.
DR   GO; GO:0009507; C:chloroplast; 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; Chloroplast; Plastid; Transferase.
FT   CHAIN           1..214
FT                   /note="Probable octanoyltransferase"
FT                   /id="PRO_0000062906"
FT   DOMAIN          30..214
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        170
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            136
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  25266 MW;  6C99FD16E800D3B2 CRC64;
     MMLIIRYGLL NFETSWVHQK TMVFIQIRKR QKKKLSIYLK HPQVYTLGHR ANKEYISFCS
     NNTLVNLHRV DRGGEVTYHD YGQVIIYNIT HLQKINRNVN IYIANLEQLG KRILLLYKTK
     STKKEKFPGI WIQQKKIVAL GIKIIQRTTF HGLSINFSCS KRNYELILAC GIKDGISVNF
     NEIHKKNSQN QFYWKYKIVL LIVDILAFNN IISF