Q04D15 (UPPP2_OENOB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Undecaprenyl-diphosphatase 2
EC=3.6.1.27

Alternative name(s):
Bacitracin resistance protein 2
Undecaprenyl pyrophosphate phosphatase 2

Gene names

Name:	uppP2
Ordered Locus Names:	OEOE_1821

Organism

Oenococcus oeni (strain ATCC BAA-331 / PSU-1) [Complete proteome] [HAMAP]

Taxonomic identifier

203123 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Oenococcus

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin By similarity. HAMAP MF_01006
Catalytic activity	Undecaprenyl diphosphate + H2O = undecaprenyl phosphate + phosphate. HAMAP MF_01006
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity HAMAP MF_01006.
Miscellaneous	Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available. HAMAP MF_01006
Sequence similarities	Belongs to the UppP family.

Ontologies

Keywords
Biological process	Antibiotic resistance Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW dephosphorylation Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	undecaprenyl-diphosphatase 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 – 271	271	Undecaprenyl-diphosphatase 2 HAMAP MF_01006		PRO_0000290740
Regions
	Transmembrane	1 – 21	21	Helical; Potential
	Transmembrane	46 – 66	21	Helical; Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Transmembrane	111 – 131	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	190 – 210	21	Helical; Potential
	Transmembrane	220 – 240	21	Helical; Potential
	Transmembrane	251 – 271	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q04D15 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 0D102F988A22A78B	FASTA	271	29,785
	10 20 30 40 50 60 MNFFQAIILA IAQGVSELFP ISSVAHSVII PYLFGWKLSP FFLKTNFLEF VVMMHIGTTI 70 80 90 100 110 120 SLIVYFRKDW KKMLKSLFNK KTSKRNLALI VIGTIPAIIL GAIFEQTITN AFSDVIVASI 130 140 150 160 170 180 FLIFNGLLLF FGEQTKKRGN KSIEDLKGWQ ALVIGCFQSL ALIPGFSRSG SSITAGFWMG 190 200 210 220 230 240 LSNEESARFS MLLSTPMVAG AATLEIPKLI KNHVPGLLSL SLIGGIVAGL AAFLSIYILM 250 260 270 HWFNHKKNNT MLPFAIYCIV IGIGVLASKA I

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-331 / PSU-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000411 Genomic DNA. Translation: ABJ57657.1.
RefSeq	YP_811322.1. NC_008528.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q04D15.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4415374.
GenomeReviews	Gene locus OEOE_1821 in contig CP000411_GR.
KEGG	ooe:OEOE_1821.
NMPDR	fig|203123.1.peg.193.
PATRIC	22801918. VBIOenOen113004_1862.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1968.
HOGENOM	HBG391969.
OMA	CLAFLPG.
PhylomeDB	Q04D15.
Family and domain databases
HAMAP	MF_01006. Undec_diphosphatase. [Tree]
InterPro	IPR003824. Bacitracin-R_BacA. [Graphical view]
KO	K06153.
Pfam	PF02673. BacA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UPPP2_OENOB

Accession

Primary (citable) accession number: Q04D15

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program