Reviewed, UniProtKB/Swiss-Prot P46130 (YBHC_ECOLI)

Names and origin

Protein names

Recommended name:
    Acyl-CoA thioester hydrolase ybgC
    EC=3.1.2.-

Gene names

Name:	ybhC
Ordered Locus Names:	b0772, JW0755

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the hydrolysis of the thioester bond in palmitoyl-CoA. Ref.8
Subcellular location	Cell outer membrane; Lipid-anchor Probable.
Sequence similarities	Belongs to the pectinesterase family.
Sequence caution	The sequence U39938 differs from that shown. Reason: Frameshift at position 37.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Lipoprotein Palmitate
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW pectinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	By similarity
	Chain	22 – 427	406	Acyl-CoA thioester hydrolase ybgC		PRO_0000023502
Sites
	Active site	285	1	Nucleophile By similarity
	Binding site	345	1	Substrate By similarity
Amino acid modifications
	Lipidation	22	1	N-palmitoyl cysteine Probable
	Lipidation	22	1	S-diacylglycerol cysteine Probable
Experimental info
	Sequence conflict	167	1	N → Q Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P46130-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 208831BE0EDBCB5C	FASTA	427	46,082
	10 20 30 40 50 60 MNTFSVSRLA LALAFGVTLT ACSSTPPDQR PSDQTAPGTS SRPILSAKEA QNFDAQHYFA 70 80 90 100 110 120 SLTPGAAAWN PSPITLPAQP DFVVGPAGTQ GVTHTTIQAA VDAAIIKRTN KRQYIAVMPG 130 140 150 160 170 180 EYQGTVYVPA APGGITLYGT GEKPIDVKIG LSLDGGMSPA DWRHDVNPRG KYMPGKPAWY 190 200 210 220 230 240 MYDSCQSKRS DSIGVLCSAV FWSQNNGLQL QNLTIENTLG DSVDAGNHPA VALRTDGDQV 250 260 270 280 290 300 QINNVNILGR QNTFFVTNSG VQNRLETNRQ PRTLVTNSYI EGDVDIVSGR GAVVFDNTEF 310 320 330 340 350 360 RVVNSRTQQE AYVFAPATLS NIYYGFLAVN SRFNAFGDGV AQLGRSLDVD ANTNGQVVIR 370 380 390 400 410 420 DSAINEGFNT AKPWADAVIS NRPFAGNTGS VDDNDEIQRN LNDTNYNRMW EYNNRGVGSK VVAEAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 33-427. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	Taylor A., Smith G.R., Gardner J.F. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-300. Strain: K12.
[5]	"Viral integration and excision: structure of the lambda att sites." Landy A., Ross W. Science 197:1147-1160(1977) [PubMed: 331474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[6]	"Detection of new genes in a bacterial genome using Markov models for three gene classes." Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A. Nucleic Acids Res. 23:3554-3562(1995) [PubMed: 7567469] [Abstract] Cited for: IDENTIFICATION.
[7]	"Proteomic analysis of the Escherichia coli outer membrane." Molloy M.P., Herbert B.R., Slade M.B., Rabilloud T., Nouwens A.S., Williams K.L., Gooley A.A. Eur. J. Biochem. 267:2871-2881(2000) [PubMed: 10806384] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"Enzyme genomics: application of general enzymatic screens to discover new enzymes." Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F. FEMS Microbiol. Rev. 29:263-279(2005) [PubMed: 15808744] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U00096 Genomic DNA. Translation: AAC73859.1.
AP009048 Genomic DNA. Translation: BAA35436.2.
U39938 Genomic DNA. No translation available.
J01638 Genomic DNA. No translation available.

PIR

D64813.

RefSeq

AP_001403.1.
NP_415293.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GRH	X-ray	1.70	A	29-427	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:11407N.

Genome annotation databases

GeneID

945381.

GenomeReviews

Gene locus JW0755 in contig AP009048_GR.
Gene locus b0772 in contig U00096_GR.

KEGG

ecj:JW0755.
eco:b0772.

Organism-specific databases

EchoBASE

EB2713.

EcoGene

EG12875. ybhC.

CMR

Search...

Phylogenomic databases

HOGENOM

P46130.

OMA

P46130. GVMCSAV.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12875-MON.

BRENDA

3.1.2.2. 246.

Family and domain databases

InterPro

IPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.

Pfam

PF01095. Pectinesterase. 1 hit.
[Graphical view]

PROSITE

PS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

YBHC_ECOLI

Accession

Primary (citable) accession number: P46130
Secondary accession number(s): P75765

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)