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Reviewed, UniProtKB/Swiss-Prot Q99T13 (Y1866_STAAM)

Last modified January 19, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Putative multidrug export ATP-binding/permease protein SAV1866
    EC=3.6.3.-
Gene names
Ordered Locus Names: SAV1866
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation. Ref.2

Enzyme regulation

ATPase activity is inhibited by orthovanadate and activated by the cancer drugs doxorubicin and vinblastine. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2.

Domain

The ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.

Sequence similarities

Belongs to the ABC transporter superfamily.

Contains 1 ABC transmembrane type-1 domain.

Contains 1 ABC transporter domain.

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Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processtransmembrane transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of substances

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Putative multidrug export ATP-binding/permease protein SAV1866
PRO_0000271549

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621 Potential
Topological domain37 – 5923Extracellular Potential
Transmembrane60 – 8021 Potential
Topological domain81 – 13858Cytoplasmic Potential
Transmembrane139 – 15921 Potential
Topological domain160 – 1623Extracellular Potential
Transmembrane163 – 18321 Potential
Topological domain184 – 24461Cytoplasmic Potential
Transmembrane245 – 26319 Potential
Topological domain264 – 2696Extracellular Potential
Transmembrane270 – 28718 Potential
Topological domain288 – 578291Cytoplasmic Potential
Domain16 – 306291ABC transmembrane type-1
Domain340 – 575236ABC transporter
Nucleotide binding374 – 3818ATP Potential

Secondary structure

1 .................................................................................... 578
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q99T13-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0DA5945AE8F1799C

FASTA57864,863
        10         20         30         40         50         60 
MIKRYLQFVK PYKYRIFATI IVGIIKFGIP MLIPLLIKYA IDGVINNHAL TTDEKVHHLT 

        70         80         90        100        110        120 
IAIGIALFIF VIVRPPIEFI RQYLAQWTSN KILYDIRKKL YNHLQALSAR FYANNQVGQV 

       130        140        150        160        170        180 
ISRVINDVEQ TKDFILTGLM NIWLDCITII IALSIMFFLD VKLTLAALFI FPFYILTVYV 

       190        200        210        220        230        240 
FFGRLRKLTR ERSQALAEVQ GFLHERVQGI SVVKSFAIED NEAKNFDKKN TNFLTRALKH 

       250        260        270        280        290        300 
TRWNAYSFAA INTVTDIGPI IVIGVGAYLA ISGSITVGTL AAFVGYLELL FGPLRRLVAS 

       310        320        330        340        350        360 
FTTLTQSFAS MDRVFQLIDE DYDIKNGVGA QPIEIKQGRI DIDHVSFQYN DNEAPILKDI 

       370        380        390        400        410        420 
NLSIEKGETV AFVGMSGGGK STLINLIPRF YDVTSGQILI DGHNIKDFLT GSLRNQIGLV 

       430        440        450        460        470        480 
QQDNILFSDT VKENILLGRP TATDEEVVEA AKMANAHDFI MNLPQGYDTE VGERGVKLSG 

       490        500        510        520        530        540 
GQKQRLSIAR IFLNNPPILI LDEATSALDL ESESIIQEAL DVLSKDRTTL IVAHRLSTIT 

       550        560        570 
HADKIVVIEN GHIVETGTHR ELIAKQGAYE HLYSIQNL

« Hide

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References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Structure of a bacterial multidrug ABC transporter."
Dawson R.J.P., Locher K.P.
Nature 443:180-185(2006) [PubMed: 16943773] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH ADP, FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB58028.1.
RefSeqNP_372390.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYDX-ray3.00A/B1-578[»]
2ONJX-ray3.40A/B1-578[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99T13.

Genome annotation databases

GeneID1121879.
GenomeReviewsGene locus SAV1866 in contig BA000017_GR.
KEGGsav:SAV1866.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1132.
HOGENOMHBG758042.
OMAIAGIADS.

Enzyme and pathway databases

BioCycSAUR158878:SAV1866-MONOMER.

Family and domain databases

InterProIPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR001140. ABC_transptr_TM_dom.
IPR011527. ABC_transptrTM_dom_typ1.
IPR003593. ATPase_AAA+_core.
[Graphical view]
PfamPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
PROSITEPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameY1866_STAAM
AccessionPrimary (citable) accession number: Q99T13
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents