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P46130 (YBHC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative acyl-CoA thioester hydrolase YbhC
EC=3.1.2.-
Gene names
Name:ybhC
Ordered Locus Names:b0772, JW0755
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative thioesterase. Does not bind pectin, and has no pectinesterase activity. Ref.8 Ref.9

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the pectinesterase family.

Caution

Lacks the conserved Asp residue in position 252 essential for pectinase activity. Likewise, most of the residues involved in substrate binding are not conserved. Was originally (Ref.8) thought to have palmitoyl-CoA thioesterase activity, but Ref.9 were unable to detect any pectinase or palmitoyl-CoA thioesterase activity. Its enzyme activity is therefore unsure.

Sequence caution

The sequence U39938 differs from that shown. Reason: Frameshift at position 37.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Chain22 – 427406Putative acyl-CoA thioester hydrolase YbhC
PRO_0000023502

Sites

Active site2851Nucleophile By similarity
Binding site3451Substrate By similarity

Amino acid modifications

Lipidation221N-palmitoyl cysteine Probable
Lipidation221S-diacylglycerol cysteine Probable
Disulfide bond185 ↔ 197 Ref.9

Experimental info

Sequence conflict1671N → Q Ref.4

Secondary structure

1 ............................................................................ 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46130 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 208831BE0EDBCB5C

FASTA42746,082
        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

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The crystal structure of the outer membrane lipoprotein YbhC from Escherichia coli sheds new light on the phylogeny of carbohydrate esterase family 8."
Ekloef J.M., Tan T.-C., Divne C., Brumer H.
Proteins 76:1029-1036(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 29-427, ABSENCE OF PECTINASE ACTIVITY, ABSENCE OF PECTIN BINDING, ABSENCE OF ACYL COENZYME A ESTERASE ACTIVITY, DISULFIDE BOND, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC73859.1.
AP009048 Genomic DNA. Translation: BAA35436.2.
U39938 Genomic DNA. No translation available.
J01638 Genomic DNA. No translation available.
PIRD64813.
RefSeqNP_415293.1. NC_000913.2.
YP_489045.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GRHX-ray1.70A29-427[»]
ProteinModelPortalP46130.
SMRP46130. Positions 29-420.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-11407N.
IntActP46130. 3 interactions.
MINTMINT-1240146.
STRING511145.b0772.

Proteomic databases

PaxDbP46130.
PRIDEP46130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73859; AAC73859; b0772.
BAA35436; BAA35436; BAA35436.
GeneID12932845.
945381.
KEGGecj:Y75_p0745.
eco:b0772.
PATRIC32116745. VBIEscCol129921_0798.

Organism-specific databases

EchoBASEEB2713.
EcoGeneEG12875. ybhC.

Phylogenomic databases

eggNOGCOG4677.
HOGENOMHOG000118057.
KOK01051.
OMAFNRMWEY.
ProtClustDBPRK10531.

Enzyme and pathway databases

BioCycEcoCyc:EG12875-MONOMER.
ECOL316407:JW0755-MONOMER.
BRENDA3.1.2.2. 2026.

Gene expression databases

GenevestigatorP46130.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46130.

Entry information

Entry nameYBHC_ECOLI
AccessionPrimary (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: May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents