YBGC_ECOLI
ID YBGC_ECOLI Reviewed; 134 AA.
AC P0A8Z3; P08999;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acyl-CoA thioester hydrolase YbgC;
DE Short=Acyl-CoA thioesterase;
DE EC=3.1.2.-;
GN Name=ybgC; OrderedLocusNames=b0736, JW0726;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3294803; DOI=10.1128/jb.169.6.2667-2674.1987;
RA Sun T.-P., Webster R.E.;
RT "Nucleotide sequence of a gene cluster involved in entry of E colicins and
RT single-stranded DNA of infecting filamentous bacteriophages into
RT Escherichia coli.";
RL J. Bacteriol. 169:2667-2674(1987).
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;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-20.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Kim K., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M.,
RA Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Komp C.,
RA Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP ACYL-COA THIOESTERASE ACTIVITY.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [8]
RP FUNCTION IN PHOSPHOLIPID METABOLISM, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH ACP; PLSB AND PSSA.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16294310; DOI=10.1002/pmic.200500115;
RA Gully D., Bouveret E.;
RT "A protein network for phospholipid synthesis uncovered by a variant of the
RT tandem affinity purification method in Escherichia coli.";
RL Proteomics 6:282-293(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RA Kim Y., Joachimiak A., Skarina T., Savchenko A., Edwards A.M.;
RT "Crystal structure of hypothetical protein Ec709 from Escherichia coli.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Thioesterase that appears to be involved in phospholipid
CC metabolism. Some specific acyl-ACPs could be physiological substrates.
CC Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro,
CC catalyzing the hydrolysis of the thioester bond.
CC {ECO:0000269|PubMed:16294310}.
CC -!- SUBUNIT: Interacts with ACP, PlsB and PssA, forming altogether a
CC complex at the inner membrane. {ECO:0000269|PubMed:16294310}.
CC -!- INTERACTION:
CC P0A8Z3; P0A6A8: acpP; NbExp=7; IntAct=EBI-543276, EBI-542566;
CC P0A8Z3; P0ADZ0: rplW; NbExp=2; IntAct=EBI-543276, EBI-542264;
CC P0A8Z3; P10408: secA; NbExp=2; IntAct=EBI-543276, EBI-543213;
CC P0A8Z3; O32591: espP; Xeno; NbExp=2; IntAct=EBI-543276, EBI-852989;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16294310}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16294310}; Cytoplasmic side
CC {ECO:0000269|PubMed:16294310}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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DR EMBL; M16489; AAA83918.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73830.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35402.1; -; Genomic_DNA.
DR EMBL; U30934; AAA74398.1; -; Genomic_DNA.
DR PIR; A25980; WMEC15.
DR RefSeq; NP_415264.1; NC_000913.3.
DR RefSeq; WP_001098384.1; NZ_STEB01000035.1.
DR PDB; 1S5U; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-134.
DR PDB; 5KL9; X-ray; 2.22 A; A/B/C/D=1-134.
DR PDB; 5T06; X-ray; 1.90 A; A/B/C/D=2-134.
DR PDB; 5T07; X-ray; 1.72 A; A/B/C/D=2-134.
DR PDBsum; 1S5U; -.
DR PDBsum; 5KL9; -.
DR PDBsum; 5T06; -.
DR PDBsum; 5T07; -.
DR AlphaFoldDB; P0A8Z3; -.
DR SMR; P0A8Z3; -.
DR BioGRID; 4259452; 197.
DR BioGRID; 853184; 1.
DR DIP; DIP-29375N; -.
DR IntAct; P0A8Z3; 11.
DR STRING; 511145.b0736; -.
DR jPOST; P0A8Z3; -.
DR PaxDb; P0A8Z3; -.
DR PRIDE; P0A8Z3; -.
DR EnsemblBacteria; AAC73830; AAC73830; b0736.
DR EnsemblBacteria; BAA35402; BAA35402; BAA35402.
DR GeneID; 67413775; -.
DR GeneID; 948907; -.
DR KEGG; ecj:JW0726; -.
DR KEGG; eco:b0736; -.
DR PATRIC; fig|1411691.4.peg.1536; -.
DR EchoBASE; EB1101; -.
DR eggNOG; COG0824; Bacteria.
DR HOGENOM; CLU_101141_7_2_6; -.
DR InParanoid; P0A8Z3; -.
DR OMA; YHASYLR; -.
DR PhylomeDB; P0A8Z3; -.
DR BioCyc; EcoCyc:EG11110-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR EvolutionaryTrace; P0A8Z3; -.
DR PRO; PR:P0A8Z3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0016790; F:thiolester hydrolase activity; IDA:EcoCyc.
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; IPR014166; Tol-Pal_acyl-CoA_thioesterase.
DR InterPro; IPR006684; YbgC/YbaW.
DR Pfam; PF03061; 4HBT; 1.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR02799; thio_ybgC; 1.
DR TIGRFAMs; TIGR00051; TIGR00051; 1.
DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..134
FT /note="Acyl-CoA thioester hydrolase YbgC"
FT /id="PRO_0000087762"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10041"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1S5U"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1S5U"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1S5U"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:1S5U"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1S5U"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1S5U"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:1S5U"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:1S5U"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:1S5U"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1S5U"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1S5U"
SQ SEQUENCE 134 AA; 15562 MW; C44582B6EC3BE989 CRC64;
MNTTLFRWPV RVYYEDTDAG GVVYHASYVA FYERARTEML RHHHFSQQAL MAERVAFVVR
KMTVEYYAPA RLDDMLEIQT EITSMRGTSL VFTQRIVNAE NTLLNEAEVL VVCVDPLKMK
PRALPKSIVA EFKQ
