LIPB_FRACC
ID LIPB_FRACC Reviewed; 221 AA.
AC Q2JB35;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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};
GN OrderedLocusNames=Francci3_2135;
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000249; ABD11507.1; -; Genomic_DNA.
DR RefSeq; WP_011436554.1; NZ_MSEA01000381.1.
DR AlphaFoldDB; Q2JB35; -.
DR SMR; Q2JB35; -.
DR STRING; 106370.Francci3_2135; -.
DR EnsemblBacteria; ABD11507; ABD11507; Francci3_2135.
DR KEGG; fra:Francci3_2135; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_3_0_11; -.
DR OMA; HMRRNIT; -.
DR OrthoDB; 1806796at2; -.
DR PhylomeDB; Q2JB35; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000001937; 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; Reference proteome; Transferase.
FT CHAIN 1..221
FT /note="Octanoyltransferase"
FT /id="PRO_0000242724"
FT DOMAIN 14..202
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 54..61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 125
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 221 AA; 24137 MW; 38F7DFE618A4C2BC CRC64;
MARMRVMVRE RIDGVRPDTL WFLSHPPVYT VGKRTPPEHR PLAGLGIPVH ETNRGGLLTY
HAPGQLVGYV MCHIGAMNAV VPFLRLLEAR LVDTVEALGI PAERRDTPPG SVELTGVWTR
RTNRKIASIG LRCTRKVTSH GFALNVDCDM RPWTWATPCG MPEVEMTSVQ RELTDAGHAV
PSMAEVREIA AEMLGARNAP HPPAPNLSSG DLGTGTRAGR T
