Reviewed, UniProtKB/Swiss-Prot P55743 (PMEB_PECCC)

Names and origin

Protein names

Recommended name:
    Pectinesterase B
      Short name=PE B
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase B

Gene names

Name:

pemB

Organism

Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)

Taxonomic identifier

555 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	178 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Pectin + n H2O = n methanol + pectate.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Cell outer membrane; Lipid-anchor By similarity.
Sequence similarities	Belongs to the pectinesterase family.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Molecular function	Aspartyl esterase Hydrolase
PTM	Lipoprotein
Gene Ontology (GO)
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membrane Inferred from electronic annotation. Source: UniProtKB-KW 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 178	›178	Pectinesterase B		PRO_0000215046
Sites
	Active site	6	1	Proton donor By similarity
	Active site	39	1	Nucleophile By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	105	1	Substrate By similarity
	Site	5	1	Transition state stabilizer By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P55743-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0366BA295279C3E8	FASTA	178	20,168
	10 20 30 40 50 60 RIGRQDTFFV NTSNLRNEYV TDRYSRAYIK DSYIEGDVDY VFGRATAVFD RVHFHTVSSR 70 80 90 100 110 120 GAKDIHVFAP DSMPWAQYGF LAVSCRFTGD EGFSGGRKAK LGRAWDQGAR QTGYQPNKTA 130 140 150 160 170 NGQLVIRDST IDASYDREQP WGVAATTARP FAGNVDSARN LDDVQFNRLW EYNNIDEV

References

[1]	Heikinheimo R., Mae A., Flego D., Pirhonen M., Koiv V., Palva E.T. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SCC3193.
[2]	Rudd K.E. Unpublished observations (JUN-1996) Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X80475 Genomic DNA. No translation available.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.11. 290410.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR018040. Pectinesterase_AS. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. Partial match. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMEB_PECCC

Accession

Primary (citable) accession number: P55743

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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