ID   LIPB_CHLAD              Reviewed;         221 AA.
AC   B8G783;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Cagg_1130;
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-66 / DSM 9485;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) 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; CP001337; ACL24040.1; -; Genomic_DNA.
DR   RefSeq; WP_012616404.1; NC_011831.1.
DR   AlphaFoldDB; B8G783; -.
DR   SMR; B8G783; -.
DR   STRING; 326427.Cagg_1130; -.
DR   EnsemblBacteria; ACL24040; ACL24040; Cagg_1130.
DR   KEGG; cag:Cagg_1130; -.
DR   eggNOG; COG0321; Bacteria.
DR   HOGENOM; CLU_035168_1_3_0; -.
DR   OMA; GEVTYHC; -.
DR   OrthoDB; 1806796at2; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000002508; 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..221
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_1000116540"
FT   DOMAIN          31..216
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        177
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         76..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         145..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         159..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   SITE            142
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ   SEQUENCE   221 AA;  23451 MW;  3F6D337C6FDC7F25 CRC64;
     MRTLTVYHLG HIDYTAAWEM QRRLARQRSS GQIGDTLLLL EHPPTITLGN KARPEHIVAT
     PAELAARGVV VVQSDRGGEV TYHAPGQLVA YPIFKLSQHG SDVGRYVRGL EESVIRVLAG
     YGITGERVNG LTGVWVRGGA AKICAIGVKL SASGVTTHGL ALNVDPDLSG FELIVPCGIS
     DRGVTSLAVE LGKAPPMAEV ADRLIASLCA IFDLRPVNAL S