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P96116 (TROA_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Periplasmic zinc-binding protein TroA
Alternative name(s):
Tromp-1
Gene names
Name:troA
Synonyms:troMP1
Ordered Locus Names:TP_0163
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of an ATP-driven transport system TroABCD for zinc. Substrate-binding protein involved in the transport of zinc across the cytoplasmic membrane.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the bacterial solute-binding protein 9 family.

Caution

Was originally (Ref.1) thought to be an outer membrane protein with porin-like properties.

Sequence caution

The sequence AAA92353.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processIon transport
Transport
Zinc transport
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: InterPro

zinc ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 308286Periplasmic zinc-binding protein TroA
PRO_0000031872

Sites

Metal binding681Zinc
Metal binding1331Zinc
Metal binding1991Zinc
Metal binding2791Zinc

Secondary structure

....................................................... 308
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96116 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 2FDD8FF20D012B08

FASTA30833,570
        10         20         30         40         50         60 
MIRERICACV LALGMLTGFT HAFGSKDAAA DGKPLVVTTI GMIADAVKNI AQGDVHLKGL 

        70         80         90        100        110        120 
MGPGVDPHLY TATAGDVEWL GNADLILYNG LHLETKMGEV FSKLRGSRLV VAVSETIPVS 

       130        140        150        160        170        180 
QRLSLEEAEF DPHVWFDVKL WSYSVKAVYE SLCKLLPGKT REFTQRYQAY QQQLDKLDAY 

       190        200        210        220        230        240 
VRRKAQSLPA ERRVLVTAHD AFGYFSRAYG FEVKGLQGVS TASEASAHDM QELAAFIAQR 

       250        260        270        280        290        300 
KLPAIFIESS IPHKNVEALR DAVQARGHVV QIGGELFSDA MGDAGTSEGT YVGMVTHNID 


TIVAALAR 

« Hide

References

« Hide 'large scale' references
[1]"Porin activity and sequence analysis of a 31-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp1)."
Blanco D.R., Champion C.I., Exner M.M., Erdjument-Bromage H., Hancock R.E., Tempst P., Miller J.N., Lovett M.A.
J. Bacteriol. 177:3556-3562(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Nichols.
[2]"Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog."
Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y., Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.
Gene 197:47-64(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Nichols.
[3]"Complete genome sequence of Treponema pallidum, the syphilis spirochete."
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. expand/collapse author list , Chidambaram M., Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., Venter J.C.
Science 281:375-388(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nichols.
[4]"Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure."
Deka R.K., Lee Y.-H., Hagman K.E., Shevchenko D., Lingwood C.A., Hasemann C.A., Norgard M.V., Radolf J.D.
J. Bacteriol. 181:4420-4423(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone."
Lee Y.-H., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A.
Nat. Struct. Biol. 6:628-633(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-313.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16363 Genomic DNA. Translation: AAA92353.1. Different initiation.
U55214 Genomic DNA. Translation: AAC45725.1.
AE000520 Genomic DNA. Translation: AAC65151.1.
PIRA71360.
RefSeqNP_218602.1. NC_000919.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0FX-ray2.50A32-308[»]
1TOAX-ray1.80A/B23-308[»]
ProteinModelPortalP96116.
SMRP96116. Positions 32-308.
ModBaseSearch...

Protein-protein interaction databases

IntActP96116. 8 interactions.
STRING243276.TP0163.

Protein family/group databases

TCDB3.A.1.15.8. ATP-binding cassette (ABC) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65151; AAC65151; TP_0163.
GeneID2611122.
KEGGtpa:TP0163.
PATRIC20530293. VBITrePal57110_0178.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0803.
KOK11707.
OMAGTYVGMM.
ProtClustDBCLSK375142.

Family and domain databases

InterProIPR006129. AdhesinB.
IPR006128. Lipoprotein_4.
IPR006127. Perip_solute-bd_prot_fam.
[Graphical view]
PfamPF01297. SBP_bac_9. 1 hit.
[Graphical view]
PRINTSPR00691. ADHESINB.
PR00690. ADHESNFAMILY.
ProtoNetSearch...

Other

EvolutionaryTraceP96116.

Entry information

Entry nameTROA_TREPA
AccessionPrimary (citable) accession number: P96116
Secondary accession number(s): Q56329
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1997
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families