YBGC_HELPY
ID YBGC_HELPY Reviewed; 133 AA.
AC P94842; O25238;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Acyl-CoA thioesterase YbgC;
DE EC=3.1.2.-;
GN Name=ybgC; OrderedLocusNames=HP_0496;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RA Clairoux N., Boissinot M.;
RT "Sequence of the dihydrodipicolinate reductase gene (dapB) from
RT Helicobacter pylori and complementation in Escherichia coli.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [3]
RP INTERACTION WITH CAGA.
RX PubMed=15133060; DOI=10.1074/mcp.m400048-mcp200;
RA Terradot L., Durnell N., Li M., Li M., Ory J., Labigne A., Legrain P.,
RA Colland F., Waksman G.;
RT "Biochemical characterization of protein complexes from the Helicobacter
RT pylori protein interaction map: strategies for complex formation and
RT evidence for novel interactions within type IV secretion systems.";
RL Mol. Cell. Proteomics 3:809-819(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=18338382; DOI=10.1002/prot.22014;
RA Angelini A., Cendron L., Goncalves S., Zanotti G., Terradot L.;
RT "Structural and enzymatic characterization of HP0496, a YbgC thioesterase
RT from Helicobacter pylori.";
RL Proteins 72:1212-1221(2008).
CC -!- FUNCTION: Thioesterase that may be involved in phospholipid metabolism.
CC Displays acyl-CoA thioesterase activity with lauroyl-CoA (C12:0),
CC myristoyl-CoA (C14:0), palmitoyl-CoA (C16:0), stearoyl-CoA (C18:0) and
CC benzoyl-CoA, catalyzing the hydrolysis of the thioester bond. Has low
CC activity with butyryl-CoA and octanoyl-CoA.
CC {ECO:0000269|PubMed:18338382}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for benzoyl-CoA;
CC KM=210 uM for stearoyl-CoA;
CC KM=570 uM for palmitoyl-CoA;
CC KM=240 uM for myristoyl-CoA;
CC KM=160 uM for lauroyl-CoA;
CC KM=40 uM for octanoyl-CoA;
CC KM=27 uM for butyryl-CoA;
CC Note=kcat is 0.028 sec(-1) with benzoyl-CoA, 0.034 sec(-1) with
CC stearoyl-CoA, 0.045 sec(-1) with palmitoyl-CoA, 0.024 sec(-1) with
CC myristoyl-CoA, 0.015 sec(-1) with lauroyl-CoA and 0.0013 sec(-1) with
CC octanoyl-CoA.;
CC -!- SUBUNIT: Homotetramer. May interact with CagA.
CC {ECO:0000269|PubMed:18338382}.
CC -!- INTERACTION:
CC P94842; P55980: cagA; NbExp=2; IntAct=EBI-528090, EBI-528104;
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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DR EMBL; U75328; AAB39716.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07561.1; -; Genomic_DNA.
DR PIR; H64581; H64581.
DR RefSeq; NP_207293.1; NC_000915.1.
DR RefSeq; WP_001203797.1; NC_018939.1.
DR PDB; 2PZH; X-ray; 1.70 A; A/B/C/D=1-133.
DR PDBsum; 2PZH; -.
DR AlphaFoldDB; P94842; -.
DR SMR; P94842; -.
DR DIP; DIP-3437N; -.
DR IntAct; P94842; 1.
DR MINT; P94842; -.
DR STRING; 85962.C694_02550; -.
DR PaxDb; P94842; -.
DR EnsemblBacteria; AAD07561; AAD07561; HP_0496.
DR KEGG; hpy:HP_0496; -.
DR PATRIC; fig|85962.47.peg.534; -.
DR eggNOG; COG0824; Bacteria.
DR OMA; FPIRVYW; -.
DR PhylomeDB; P94842; -.
DR EvolutionaryTrace; P94842; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR008272; HB-CoA_thioesterase_AS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR InterPro; IPR006684; YbgC/YbaW.
DR Pfam; PF03061; 4HBT; 1.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00051; TIGR00051; 1.
DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lipid metabolism; Reference proteome.
FT CHAIN 1..133
FT /note="Acyl-CoA thioesterase YbgC"
FT /id="PRO_0000087767"
FT ACT_SITE 11
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10041"
FT CONFLICT 133
FT /note="I -> V (in Ref. 1; AAB39716)"
FT /evidence="ECO:0000305"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:2PZH"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2PZH"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2PZH"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 77..90
FT /evidence="ECO:0007829|PDB:2PZH"
FT STRAND 100..112
FT /evidence="ECO:0007829|PDB:2PZH"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2PZH"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2PZH"
SQ SEQUENCE 133 AA; 15596 MW; 18C969BB96B802F9 CRC64;
MRCRVYYEDT DSEGVVYHAN YLKYCERARS EFFFKQNVLP ENEEGVFVIR SIKADFFTPA
SLGQVLEIRT QIKELRKVFV VLFQEIYCIQ NASLEPMKPF KVFASEIKFG FVNRSTYSPI
AIPKLFKELL NAI
