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Q3MFH9

- UPPP_ANAVT

UniProt

Q3MFH9 - UPPP_ANAVT

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Protein

Undecaprenyl-diphosphatase

Gene

uppP

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
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

BioCyciAVAR240292:GCY3-636-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:Ava_0633
OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
Taxonomic identifieri240292 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena
ProteomesiUP000002533: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalUniRule annotationAdd
BLAST
Transmembranei82 – 10221HelicalUniRule annotationAdd
BLAST
Transmembranei130 – 15021HelicalUniRule annotationAdd
BLAST
Transmembranei161 – 18121HelicalUniRule annotationAdd
BLAST
Transmembranei191 – 21121HelicalUniRule annotationAdd
BLAST
Transmembranei236 – 25621HelicalUniRule annotationAdd
BLAST
Transmembranei265 – 28521HelicalUniRule annotationAdd
BLAST
Transmembranei296 – 31621HelicalUniRule annotationAdd
BLAST

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 – 320320Undecaprenyl-diphosphatasePRO_0000250223Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi240292.Ava_0633.

Family & Domainsi

Sequence similaritiesi

Belongs to the UppP family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1968.
HOGENOMiHOG000218357.
KOiK06153.
OMAiKENTAIQ.
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.

Q3MFH9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLFKRQWFV LVSAVSAALS VVLFPLEVFS ASPNSVGGGV QQMNILQAIV
60 70 80 90 100
LGFVQGMTEF LPISSTAHLK VVPVALGWGD PGVAFTAIIQ LGSIAAVLWY
110 120 130 140 150
FWGDLTRIIK GATRAIALKD YADYDLRLSL GIILGTIPIV FFGLLIKKLI
160 170 180 190 200
PDFDSSPIRS LGAIAVASIV MSLLLGVGEK LGKRERDFEH LTMQDGLLMG
210 220 230 240 250
LAQALALIPG VSRSGSTLTS GLFMGLQRET AARFSFLLGI PAITLAGLVE
260 270 280 290 300
LKDVFAEGIA DGAALPLIVG VISAAIFSYM AIAGLLSFLK TQSTWVFIWY
310 320
RLVFGIAILG AISAGILQNS
Length:320
Mass (Da):33,975
Last modified:October 25, 2005 - v1
Checksum:iDA9BE946B4C997E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA20257.1.
RefSeqiYP_321152.1. NC_007413.1.

Genome annotation databases

EnsemblBacteriaiABA20257; ABA20257; Ava_0633.
GeneIDi3678662.
KEGGiava:Ava_0633.
PATRICi35421658. VBIAnaVar43351_1400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA20257.1 .
RefSeqi YP_321152.1. NC_007413.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 240292.Ava_0633.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABA20257 ; ABA20257 ; Ava_0633 .
GeneIDi 3678662.
KEGGi ava:Ava_0633.
PATRICi 35421658. VBIAnaVar43351_1400.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci AVAR240292:GCY3-636-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 Anabaena variabilis ATCC 29413."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29413 / PCC 7937.

Entry informationi

Entry nameiUPPP_ANAVT
AccessioniPrimary (citable) accession number: Q3MFH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 25, 2005
Last modified: November 26, 2014
This is version 63 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3