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Q9K0Z3 (UPPP_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Undecaprenyl-diphosphatase

EC=3.6.1.27
Alternative name(s):
Bacitracin resistance protein
Undecaprenyl pyrophosphate phosphatase
Gene names
Name:uppP
Synonyms:bacA, upk
Ordered Locus Names:NMB0408
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin By similarity. HAMAP-Rule MF_01006

Catalytic activity

Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate. HAMAP-Rule MF_01006

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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.

Sequence similarities

Belongs to the UppP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Undecaprenyl-diphosphatase HAMAP-Rule MF_01006
PRO_0000151169

Regions

Transmembrane13 – 3523Helical; Potential
Transmembrane45 – 6218Helical; Potential
Transmembrane82 – 10221Helical; Potential
Transmembrane108 – 12821Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane219 – 23921Helical; Potential
Transmembrane250 – 27021Helical; Potential

Experimental info

Sequence conflict381G → D in AAO85431. Ref.1
Sequence conflict731L → V in AAO85431. Ref.1
Sequence conflict1071Y → H in AAO85431. Ref.1
Sequence conflict2401R → K in AAO85431. Ref.1
Sequence conflict2601A → V in AAO85431. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9K0Z3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0976868A46AF8FAA

FASTA27330,371
        10         20         30         40         50         60 
MDFLIVLKAL MMGLVEGFTE FLPISSTGHL IVFGNLIGFH SNHKVFEIAI QLGAVLAVVF 

        70         80         90        100        110        120 
EYRQRFSNVL HGLGKDRKAN RFVLNLAIAF IPAAVMGLLF GKQIKEYLFN PLSVAVMLVL 

       130        140        150        160        170        180 
GGFFILWVEK RQSRAEPKIA DVDALRPIDA LMIGVAQVFA LVPGTSRSGS TIMGGMLWGI 

       190        200        210        220        230        240 
ERKTATEFSF FLAVPMMVAA TAYDVLKHYR FFTLHDVGLI LIGFIAAFVS GLVAVKALLR 

       250        260        270 
FVSKKNYIPF AYYRIVFGIA IIILWLSGWI SWE 

« Hide

References

« Hide 'large scale' references
[1]"BacA is involved in the assembly of the alpha-chain oligosaccharide in Neisseria meningitidis serogroup B."
Post D.M.B., Zaleski A., Gibson B.W., Apicella M.A.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NMB / Serogroup B.
[2]"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58."
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. expand/collapse author list , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.
Science 287:1809-1815(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF469607 Genomic DNA. Translation: AAO85431.1.
AE002098 Genomic DNA. Translation: AAF40847.1.
PIRE81203.
RefSeqNP_273457.1. NC_003112.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB0408.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF40847; AAF40847; NMB0408.
GeneID902522.
KEGGnme:NMB0408.
PATRIC20355999. VBINeiMen85645_0517.

Phylogenomic databases

eggNOGCOG1968.
HOGENOMHOG000218356.
KOK06153.
OMAFNDAHAK.
OrthoDBEOG6QP13M.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-430-MONOMER.

Family and domain databases

HAMAPMF_01006. Undec_diphosphatase.
InterProIPR003824. UppP.
[Graphical view]
PfamPF02673. BacA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00753. undec_PP_bacA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUPPP_NEIMB
AccessionPrimary (citable) accession number: Q9K0Z3
Secondary accession number(s): Q84BX2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families