ID   LIPL_BACVZ              Reviewed;         287 AA.
AC   A7Z9Y5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE            EC=2.3.1.204 {ECO:0000255|HAMAP-Rule:MF_02119};
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN   Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119}; Synonyms=ywfL;
GN   OrderedLocusNames=RBAM_034820;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC       moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC         Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC         Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02119};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC       {ECO:0000255|HAMAP-Rule:MF_02119}.
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DR   EMBL; CP000560; ABS75811.1; -; Genomic_DNA.
DR   RefSeq; WP_012118702.1; NC_009725.2.
DR   AlphaFoldDB; A7Z9Y5; -.
DR   SMR; A7Z9Y5; -.
DR   STRING; 326423.RBAM_034820; -.
DR   EnsemblBacteria; ABS75811; ABS75811; RBAM_034820.
DR   KEGG; bay:RBAM_034820; -.
DR   HOGENOM; CLU_067270_0_0_9; -.
DR   OMA; VQIYLCI; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_02119; LipL; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024897; LipL.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..287
FT                   /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT                   /id="PRO_0000410833"
FT   DOMAIN          45..253
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT   SITE            162
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   287 AA;  32170 MW;  3F05F9D1067E3186 CRC64;
     MGKQPIDLLM QPSWRIIDQS SLGPYFDAKQ SFAMDDTLCA SVGKGESPAT ARSWVHHRTI
     VLGIQDTRLP FLEDGVKLLE DEGYRVIVRN SGGLAVVLDE GVLNISLIFE DEKKGIDIDR
     GYEAMTELVR RMLRPHHAEI EAYEIKGSYC PGSYDLSIGG RKFAGISQRR LRGGTAVQIY
     LCADKSGSER ADLIRRFYQA ALKDKSNDTK GVYPDIRPET MASLSELLRT DITVQDLMLA
     LLTELKELSG RLYAAGLSPE EEMVFEKNLT RMLERNEKVF GTQESLD