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Database: UniProt
Entry: A0A1M5JYC2_9GAMM
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ID   A0A1M5JYC2_9GAMM        Unreviewed;       220 AA.
AC   A0A1M5JYC2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN04488068_0261 {ECO:0000313|EMBL:SHG45385.1};
OS   Hydrocarboniphaga daqingensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=490188 {ECO:0000313|EMBL:SHG45385.1, ECO:0000313|Proteomes:UP000199758};
RN   [1] {ECO:0000313|EMBL:SHG45385.1, ECO:0000313|Proteomes:UP000199758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7049 {ECO:0000313|EMBL:SHG45385.1,
RC   ECO:0000313|Proteomes:UP000199758};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQWZ01000001; SHG45385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5JYC2; -.
DR   STRING; 490188.SAMN04488068_0261; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000199758; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000199758};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00013}.
FT   DOMAIN          38..216
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        179
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-1"
FT   BINDING         77..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         148..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         161..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   SITE            145
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-3"
SQ   SEQUENCE   220 AA;  23898 MW;  4D7EACD85F48F672 CRC64;
     MANNAGDGGA PQLRELPGLT DYALSAEQMR GFTETRTADT EDEIWLLQHP PVFTQGQAGR
     DEHLLMPGDI PVVRSNRGGQ VTYHGPGQIV AYLMIDLHRA GYGIRSLVTR IEDALITTLA
     GYGISAYSDP DARGVYVDID GRRHKIASLG LRVSRGCSYH GLALNTDMDL EPFTRINPCG
     YQGLRVTQVR DLGGPSLPQV QADLGRHLQR AVRMPAAPPA
//
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