LIPB_PORGI
ID LIPB_PORGI Reviewed; 492 AA.
AC Q7MUY1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=PG_1343;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LipB family.
CC {ECO:0000305}.
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DR EMBL; AE015924; AAQ66409.1; -; Genomic_DNA.
DR RefSeq; WP_005874064.1; NC_002950.2.
DR AlphaFoldDB; Q7MUY1; -.
DR SMR; Q7MUY1; -.
DR STRING; 242619.PG_1343; -.
DR EnsemblBacteria; AAQ66409; AAQ66409; PG_1343.
DR KEGG; pgi:PG_1343; -.
DR eggNOG; COG0321; Bacteria.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_053840_0_0_10; -.
DR OMA; LFCEHEP; -.
DR OrthoDB; 1712770at2; -.
DR BioCyc; PGIN242619:G1G02-1248-MON; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..492
FT /note="Octanoyltransferase"
FT /id="PRO_0000062861"
FT DOMAIN 305..492
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT REGION 1..255
FT /note="Unknown"
FT REGION 256..492
FT /note="LipB domain"
FT ACT_SITE 454
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 350..357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 423..425
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 436..438
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 420
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 492 AA; 55795 MW; 422BEDFB4466E79B CRC64;
MRCILLGSGT STGVPEVGCH CRVCRSEDRH DKRTRTSLLI ITDAGKRILI DCSPDFRQQA
LFAGIDSLDA VLLTHEHFDH VGGLDDLRTI CWHRELAVYA EQNVLDSIRD RLHYVFRKNP
YPGTPLLKLC EVKPDMPFQV ADLTVEPLRI MHGRLPILGY KIGEMAFLTD MKDIAAEEIE
CLKSCRLLFI NGLRYRKEHP SHQTIEQAID TIGQIGNPES VLIHLSHHAP LHQEHLEILP
PHIHSGYDGL EAIIDEKGIR IKDFEPHVSR SEYHYQDCGR IGYESALTLQ RKLFHDAVAD
KLENRKPQNT LLFCEHEPVL TLGKHGHEEN LLLSESELKS RDIRLFHIER GGDITYHGPG
QITGYPIFDL EQYGIGLRSY IEMLEQCIID LIAIFGLKGE RSAGASGVWL DPDIPGRTRK
ICAIGVKSSR HITMHGFALN VNTDLDYFKL INPCGFSDRG VTSISRELGR EQDFILVKQQ
LEAVFRRNFG AL
