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Entry: A0A0B0DF95_9MICC
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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
//
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