ID A0A0B0DF95_9MICC Unreviewed; 245 AA.
AC A0A0B0DF95;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013};
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=AS25_03210 {ECO:0000313|EMBL:KHE74842.1};
OS Kocuria marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE74842.1, ECO:0000313|Proteomes:UP000030664};
RN [1] {ECO:0000313|EMBL:KHE74842.1, ECO:0000313|Proteomes:UP000030664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO9-6 {ECO:0000313|EMBL:KHE74842.1,
RC ECO:0000313|Proteomes:UP000030664};
RA Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA Ottoboni L.M.;
RT "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT actinobacterium isolated from a copper mine.";
RL Submitted (SEP-2014) 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 -!- 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};
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}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHE74842.1}.
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DR EMBL; JROM01000016; KHE74842.1; -; Genomic_DNA.
DR RefSeq; WP_035961356.1; NZ_JROM01000016.1.
DR AlphaFoldDB; A0A0B0DF95; -.
DR STRING; 223184.AS25_03210; -.
DR eggNOG; COG0321; Bacteria.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000030664; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 NCBIfam; TIGR00214; lipB; 1.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00013}.
FT DOMAIN 34..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 219..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 72..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 157..159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT SITE 141
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
SQ SEQUENCE 245 AA; 26720 MW; 25C9422A213B58F6 CRC64;
MALHFERIGL APDFVNYREC LDLQREVHGE VVAGTRGNTV LMVEHEPVYT AGRRTEKHEY
PWDGTDVVPI GRGGKLTYHG PGMLVGYPIV RLPIPLDVVR FVRVLEEVII AVVREFGVPA
TTVEGRSGAW VLADERGPDR KISAIGVQVS KRATMHGFAL NCSNDLRPFG KIIPCGITDA
GVTSISQETG NRIDPADVVQ RMEQELAARE ADLCVPFEPD VPAPPVQLPH TGDSRARDAT
PTAVS
//