LIPL_BACSU
ID LIPL_BACSU Reviewed; 281 AA.
AC P39648;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase;
DE EC=2.3.1.204;
DE AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase;
GN Name=lipL; Synonyms=ywfL; OrderedLocusNames=BSU37640; ORFNames=ipa-90d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP GENE NAME, ROLE IN PROTEIN LIPOYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=21338420; DOI=10.1111/j.1365-2958.2011.07597.x;
RA Martin N., Christensen Q.H., Mansilla M.C., Cronan J.E., de Mendoza D.;
RT "A novel two-gene requirement for the octanoyltransfer reaction of Bacillus
RT subtilis lipoic acid biosynthesis.";
RL Mol. Microbiol. 80:335-349(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-39; CYS-150 AND TYR-180.
RC STRAIN=168 / JH642;
RX PubMed=21338421; DOI=10.1111/j.1365-2958.2011.07598.x;
RA Christensen Q.H., Martin N., Mansilla M.C., de Mendoza D., Cronan J.E.;
RT "A novel amidotransferase required for lipoic acid cofactor assembly in
RT Bacillus subtilis.";
RL Mol. Microbiol. 80:350-363(2011).
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:0000269|PubMed:21338420,
CC ECO:0000269|PubMed:21338421}.
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;
CC Evidence={ECO:0000269|PubMed:21338421};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein].
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in
CC minimal medium. Addition of lipoic acid only partially restores growth
CC of the mutant strain but the double mutant strain lacking both lipL and
CC lplJ fails to grow in minimal medium containing lipoic acid. Moreover,
CC the lipL mutant cells grow as well as wild-type in minimal medium
CC supplemented with acetate and BCFA precursors.
CC {ECO:0000269|PubMed:21338420}.
CC -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC intermediate.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51646.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15791.1; -; Genomic_DNA.
DR PIR; S39745; S39745.
DR RefSeq; NP_391644.1; NC_000964.3.
DR RefSeq; WP_003227511.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39648; -.
DR SMR; P39648; -.
DR STRING; 224308.BSU37640; -.
DR PaxDb; P39648; -.
DR PRIDE; P39648; -.
DR EnsemblBacteria; CAB15791; CAB15791; BSU_37640.
DR GeneID; 937083; -.
DR KEGG; bsu:BSU37640; -.
DR PATRIC; fig|224308.179.peg.4076; -.
DR eggNOG; COG0095; Bacteria.
DR OMA; VQIYLCI; -.
DR PhylomeDB; P39648; -.
DR BioCyc; BSUB:BSU37640-MON; -.
DR BioCyc; MetaCyc:BSU37640-MON; -.
DR BRENDA; 2.3.1.204; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016415; F:octanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009107; P:lipoate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..281
FT /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT /id="PRO_0000049972"
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:0000269|PubMed:21338421"
FT SITE 162
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="C->A,S: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:21338421"
FT MUTAGEN 150
FT /note="C->A,S: Loss of catalytic activity. Unable to form
FT an octanoyl-enzyme intermediate."
FT /evidence="ECO:0000269|PubMed:21338421"
FT MUTAGEN 180
FT /note="Y->A,F: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:21338421"
SQ SEQUENCE 281 AA; 31424 MW; B17CA2E1855B047E CRC64;
MANQPIDLLM QPKWRVIDQS SLGPLFDAKQ SFAMDDTLCM SVGKGVSPAT ARSWVHHDTI
VLGIQDTRLP FLQDGISLLE SEGYRVIVRN SGGLAVVLDD GVLNISLIFE DEKKGIDIDK
GYEAMVELMR RMLRPYNAKI EAYEIEGSYC PGSYDLSING KKFAGISQRR VRGGVAVQIY
LCADKSGSER ADLIRRFYQA ALKDKQNDKK GVYPEIRPET MASLSELLQK DISVQDLMFA
LLTELKALST HLYSAGLSID EEMEFEKNLV RMAERNAKVF G
