LIPB_ECOLI
ID LIPB_ECOLI Reviewed; 213 AA.
AC P60720; P30976; P77684; Q8XBQ2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013};
GN OrderedLocusNames=b0630, JW5089;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8444795; DOI=10.1128/jb.175.5.1325-1336.1993;
RA Reed K.E., Cronan J.E. Jr.;
RT "Lipoic acid metabolism in Escherichia coli: sequencing and functional
RT characterization of the lipA and lipB genes.";
RL J. Bacteriol. 175:1325-1336(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / JK1;
RX PubMed=8002607; DOI=10.1128/jb.177.1.1-10.1995;
RA Morris T.W., Reed K.E., Cronan J.E. Jr.;
RT "Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define
RT redundant pathways for ligation of lipoyl groups to apoprotein.";
RL J. Bacteriol. 177:1-10(1995).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=K12 / JK1;
RX PubMed=12591875; DOI=10.1128/jb.185.5.1582-1589.2003;
RA Jordan S.W., Cronan J.E. Jr.;
RT "The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier
RT protein:protein transferase.";
RL J. Bacteriol. 185:1582-1589(2003).
RN [8]
RP FUNCTION, REACTION INTERMEDIATE, MUTAGENESIS OF CYS-169, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=K12 / JK1;
RX PubMed=16342964; DOI=10.1021/bi051865y;
RA Zhao X., Miller J.R., Cronan J.E. Jr.;
RT "The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-
RT octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-
RT enzyme intermediate.";
RL Biochemistry 44:16737-16746(2005).
RN [9]
RP FUNCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15642479; DOI=10.1016/j.pep.2004.10.021;
RA Nesbitt N.M., Baleanu-Gogonea C., Cicchillo R.M., Goodson K., Iwig D.F.,
RA Broadwater J.A., Haas J.A., Fox B.G., Booker S.J.;
RT "Expression, purification, and physical characterization of Escherichia
RT coli lipoyl(octanoyl)transferase.";
RL Protein Expr. Purif. 39:269-282(2005).
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:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:15642479,
CC ECO:0000269|PubMed:16342964}.
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:0000255|HAMAP-Rule:MF_00013};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 uM for octanoyl-ACP {ECO:0000269|PubMed:15642479};
CC KM=13.2 uM for apo-H protein {ECO:0000269|PubMed:15642479};
CC pH dependence:
CC Optimum pH is about 7.5. {ECO:0000269|PubMed:15642479};
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:0000255|HAMAP-Rule:MF_00013}.
CC -!- SUBUNIT: Monomer or homotrimer. Both forms are active.
CC {ECO:0000269|PubMed:15642479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- MASS SPECTROMETRY: Mass=23880.45; Mass_error=1.31; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15642479};
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 -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC Rule:MF_00013}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA66342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB40830.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L07636; AAA66342.1; ALT_INIT; Genomic_DNA.
DR EMBL; U82598; AAB40830.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73731.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35273.2; -; Genomic_DNA.
DR PIR; D64797; D64797.
DR RefSeq; NP_415163.2; NC_000913.3.
DR RefSeq; WP_000284027.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P60720; -.
DR SMR; P60720; -.
DR BioGRID; 4261534; 35.
DR STRING; 511145.b0630; -.
DR jPOST; P60720; -.
DR PaxDb; P60720; -.
DR PRIDE; P60720; -.
DR EnsemblBacteria; AAC73731; AAC73731; b0630.
DR EnsemblBacteria; BAA35273; BAA35273; BAA35273.
DR GeneID; 66671096; -.
DR GeneID; 945217; -.
DR KEGG; ecj:JW5089; -.
DR KEGG; eco:b0630; -.
DR PATRIC; fig|1411691.4.peg.1638; -.
DR EchoBASE; EB1283; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_3_1_6; -.
DR InParanoid; P60720; -.
DR OMA; GEVTYHC; -.
DR PhylomeDB; P60720; -.
DR BioCyc; EcoCyc:EG11591-MON; -.
DR BioCyc; MetaCyc:EG11591-MON; -.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:P60720; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IDA:EcoliWiki.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IDA:EcoCyc.
DR GO; GO:0016415; F:octanoyltransferase activity; IMP:EcoCyc.
DR GO; GO:0016740; F:transferase activity; IDA:EcoliWiki.
DR GO; GO:0009107; P:lipoate biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009106; P:lipoate metabolic process; IMP:EcoliWiki.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:EcoliWiki.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 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 PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="Octanoyltransferase"
FT /id="PRO_0000062834"
FT DOMAIN 32..207
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 169
FT /note="Acyl-thioester intermediate"
FT BINDING 71..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 138..140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 151..153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 135
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT MUTAGEN 137
FT /note="C->A: No effect on activity."
FT MUTAGEN 147
FT /note="C->A: No effect on activity."
FT MUTAGEN 169
FT /note="C->A: 1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16342964"
FT MUTAGEN 169
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16342964"
FT CONFLICT 33
FT /note="S -> D (in Ref. 1; AAA66342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23883 MW; 56EE2BB105F99EAD CRC64;
MYQDKILVRQ LGLQPYEPIS QAMHEFTDTR DDSTLDEIWL VEHYPVFTQG QAGKAEHILM
PGDIPVIQSD RGGQVTYHGP GQQVMYVLLN LKRRKLGVRE LVTLLEQTVV NTLAELGIEA
HPRADAPGVY VGEKKICSLG LRIRRGCSFH GLALNVNMDL SPFLRINPCG YAGMEMAKIS
QWKPEATTNN IAPRLLENIL ALLNNPDFEY ITA
