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B4SDS7

- UPPP_PELPB

UniProt

B4SDS7 - UPPP_PELPB

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Protein

Undecaprenyl-diphosphatase

Gene

uppP

Organism
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.UniRule annotation

Catalytic activityi

Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.UniRule annotation

GO - Molecular functioni

  1. undecaprenyl-diphosphatase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. dephosphorylation Source: InterPro
  3. peptidoglycan biosynthetic process Source: UniProtKB-KW
  4. regulation of cell shape Source: UniProtKB-KW
  5. response to antibiotic Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciPPHA324925:GHBF-2294-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Undecaprenyl-diphosphataseUniRule annotation (EC:3.6.1.27UniRule annotation)
Alternative name(s):
Bacitracin resistance proteinUniRule annotation
Undecaprenyl pyrophosphate phosphataseUniRule annotation
Gene namesi
Name:uppPUniRule annotation
Ordered Locus Names:Ppha_2250
OrganismiPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Taxonomic identifieri324925 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon
ProteomesiUP000002724: Chromosome

Subcellular locationi

Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Undecaprenyl-diphosphatasePRO_1000197386Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi324925.Ppha_2250.

Structurei

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei51 – 7121HelicalUniRule annotationAdd
BLAST
Transmembranei87 – 10721HelicalUniRule annotationAdd
BLAST
Transmembranei115 – 13521HelicalUniRule annotationAdd
BLAST
Transmembranei191 – 21121HelicalUniRule annotationAdd
BLAST
Transmembranei229 – 24921HelicalUniRule annotationAdd
BLAST
Transmembranei259 – 27921HelicalUniRule annotationAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the UppP family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1968.
HOGENOMiHOG000218357.
KOiK06153.
OMAiMENIGWK.
OrthoDBiEOG6QP13M.

Family and domain databases

HAMAPiMF_01006. Undec_diphosphatase.
InterProiIPR003824. UppP.
[Graphical view]
PfamiPF02673. BacA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00753. undec_PP_bacA. 1 hit.

Sequencei

Sequence statusi: Complete.

B4SDS7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLFEAIVLG IVQGLTEFLP ISSTAHLRII PALAGWEDPG AAFTAIVQIG
60 70 80 90 100
TLVAVLLYFW KDIFIIVAAV IEGIVQRKPL ENSDAKMGWM IVAGTIPIVI
110 120 130 140 150
FGKLFETQID TTLRSLYWIS GSLIGLAIIL FLAEGKIKNR IKKELPLKAM
160 170 180 190 200
ENIGWKEALL IGLAQSIALI PGSSRSGVTI TGGLFLNLDR ATAARFSFLL
210 220 230 240 250
SLPAVFAAGL YKLYQTWDII VASPEHITNI LVATLVAGIV GYASIAFLLN
260 270 280
YLKKHTTTIF IAYRLVAGTA ILYLVATGVL QP
Length:282
Mass (Da):30,512
Last modified:September 23, 2008 - v1
Checksum:i100092AA74CD5C54
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001110 Genomic DNA. Translation: ACF44445.1.
RefSeqiYP_002019062.1. NC_011060.1.

Genome annotation databases

EnsemblBacteriaiACF44445; ACF44445; Ppha_2250.
GeneIDi6462056.
KEGGipph:Ppha_2250.
PATRICi22905267. VBIPelPha134556_2399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001110 Genomic DNA. Translation: ACF44445.1 .
RefSeqi YP_002019062.1. NC_011060.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 324925.Ppha_2250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF44445 ; ACF44445 ; Ppha_2250 .
GeneIDi 6462056.
KEGGi pph:Ppha_2250.
PATRICi 22905267. VBIPelPha134556_2399.

Phylogenomic databases

eggNOGi COG1968.
HOGENOMi HOG000218357.
KOi K06153.
OMAi MENIGWK.
OrthoDBi EOG6QP13M.

Enzyme and pathway databases

BioCyci PPHA324925:GHBF-2294-MONOMER.

Family and domain databases

HAMAPi MF_01006. Undec_diphosphatase.
InterProi IPR003824. UppP.
[Graphical view ]
Pfami PF02673. BacA. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00753. undec_PP_bacA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5477 / BU-1.

Entry informationi

Entry nameiUPPP_PELPB
AccessioniPrimary (citable) accession number: B4SDS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: October 29, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3