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Database: UniProt
Entry: E0ICG9_9BACL
LinkDB: E0ICG9_9BACL
Original site: E0ICG9_9BACL 
ID   E0ICG9_9BACL            Unreviewed;       245 AA.
AC   E0ICG9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
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=PaecuDRAFT_3358 {ECO:0000313|EMBL:EFM09855.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM09855.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM09855.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM09855.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-2010) 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:0000256|ARBA:ARBA00024732, ECO:0000256|HAMAP-Rule:MF_00013,
CC       ECO:0000256|PIRNR:PIRNR016262}.
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:0000256|ARBA:ARBA00000953, ECO:0000256|HAMAP-
CC         Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
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|ARBA:ARBA00004821, ECO:0000256|HAMAP-
CC       Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00013}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
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DR   EMBL; AEDD01000009; EFM09855.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0ICG9; -.
DR   STRING; 717606.PaecuDRAFT_3358; -.
DR   eggNOG; COG0321; Bacteria.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000005387; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16444; LipB; 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   NCBIfam; TIGR00214; lipB; 1.
DR   PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013};
KW   Ligase {ECO:0000313|EMBL:EFM09855.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00013}.
FT   DOMAIN          38..228
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        189
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-1"
FT   BINDING         83..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         150..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         169..171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   SITE            147
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-3"
SQ   SEQUENCE   245 AA;  26876 MW;  F00F47184A2901B5 CRC64;
     MTITTQSDRL LTARYIPLIG YAEAWELQKS YVTGIDKEEQ SETLLLLQHP PTYTLGSDRH
     PEHLLLDEAQ LQEQGISVFE IDRGGDITYH GPGQLVGYPL LYLPAEGLDL HGYLRQLEQV
     IIDWLAGYGV EGGRKEAYTG VWVGHSKIAA IGVKFNRART RRGFVTSHGF ALNLKAGIGD
     EGFQGIVPCG ITEYGVTSFE DLTGLTMSPE RAAEELLPLF CRQFGCVAPS GLLSDKHPAD
     AGDND
//
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