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Protein

Putative multidrug export ATP-binding/permease protein SAV1866

Gene

SAV1866

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

ATPase activity is inhibited by orthovanadate and activated by the cancer drugs doxorubicin and vinblastine.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi374 – 3818ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1921-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative multidrug export ATP-binding/permease protein SAV1866 (EC:3.6.3.-)
Gene namesi
Ordered Locus Names:SAV1866
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein PROSITE-ProRule annotation1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence analysisAdd
BLAST
Transmembranei16 – 3621HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini37 – 5923ExtracellularSequence analysisAdd
BLAST
Transmembranei60 – 8021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini81 – 13858CytoplasmicSequence analysisAdd
BLAST
Transmembranei139 – 15921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini160 – 1623ExtracellularSequence analysis
Transmembranei163 – 18321HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini184 – 24461CytoplasmicSequence analysisAdd
BLAST
Transmembranei245 – 26319HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini264 – 2696ExtracellularSequence analysis
Transmembranei270 – 28718HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini288 – 578291CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578Putative multidrug export ATP-binding/permease protein SAV1866PRO_0000271549Add
BLAST

Proteomic databases

PaxDbiQ99T13.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-60414N.
STRINGi158878.SAV1866.

Structurei

Secondary structure

1
578
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 98Combined sources
Helixi10 – 123Combined sources
Helixi13 – 2412Combined sources
Turni25 – 273Combined sources
Helixi28 – 4417Combined sources
Helixi52 – 7221Combined sources
Helixi74 – 10633Combined sources
Helixi109 – 1135Combined sources
Helixi117 – 13014Combined sources
Helixi132 – 1365Combined sources
Helixi137 – 1415Combined sources
Helixi142 – 15918Combined sources
Turni161 – 1633Combined sources
Helixi164 – 1674Combined sources
Helixi170 – 21546Combined sources
Helixi219 – 27254Combined sources
Helixi277 – 2859Combined sources
Helixi287 – 2904Combined sources
Helixi293 – 31826Combined sources
Beta strandi340 – 3478Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi356 – 3649Combined sources
Beta strandi369 – 3735Combined sources
Helixi380 – 3845Combined sources
Turni385 – 3895Combined sources
Beta strandi394 – 4007Combined sources
Helixi405 – 4073Combined sources
Helixi410 – 4156Combined sources
Beta strandi417 – 4204Combined sources
Beta strandi428 – 4303Combined sources
Helixi431 – 4355Combined sources
Helixi436 – 4383Combined sources
Helixi444 – 45310Combined sources
Helixi457 – 4615Combined sources
Helixi466 – 4683Combined sources
Helixi473 – 4753Combined sources
Helixi480 – 49415Combined sources
Beta strandi497 – 5037Combined sources
Turni504 – 5074Combined sources
Helixi510 – 52314Combined sources
Turni524 – 5263Combined sources
Beta strandi527 – 5326Combined sources
Helixi536 – 5383Combined sources
Turni539 – 5413Combined sources
Beta strandi543 – 5497Combined sources
Beta strandi552 – 5576Combined sources
Helixi559 – 5646Combined sources
Helixi568 – 5736Combined sources
Turni574 – 5774Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYDX-ray3.00A/B1-578[»]
2ONJX-ray3.40A/B1-578[»]
4A82electron microscopy2.00A/B/C/D1-578[»]
ProteinModelPortaliQ99T13.
SMRiQ99T13. Positions 1-578.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99T13.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 306291ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 575236ABC transporterPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ABC transporter superfamily.Curated
Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZ1. Bacteria.
COG1132. LUCA.
KOiK11085.
OMAiAISHTNW.
OrthoDBiEOG6T7N3V.
PhylomeDBiQ99T13.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99T13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKRYLQFVK PYKYRIFATI IVGIIKFGIP MLIPLLIKYA IDGVINNHAL
60 70 80 90 100
TTDEKVHHLT IAIGIALFIF VIVRPPIEFI RQYLAQWTSN KILYDIRKKL
110 120 130 140 150
YNHLQALSAR FYANNQVGQV ISRVINDVEQ TKDFILTGLM NIWLDCITII
160 170 180 190 200
IALSIMFFLD VKLTLAALFI FPFYILTVYV FFGRLRKLTR ERSQALAEVQ
210 220 230 240 250
GFLHERVQGI SVVKSFAIED NEAKNFDKKN TNFLTRALKH TRWNAYSFAA
260 270 280 290 300
INTVTDIGPI IVIGVGAYLA ISGSITVGTL AAFVGYLELL FGPLRRLVAS
310 320 330 340 350
FTTLTQSFAS MDRVFQLIDE DYDIKNGVGA QPIEIKQGRI DIDHVSFQYN
360 370 380 390 400
DNEAPILKDI NLSIEKGETV AFVGMSGGGK STLINLIPRF YDVTSGQILI
410 420 430 440 450
DGHNIKDFLT GSLRNQIGLV QQDNILFSDT VKENILLGRP TATDEEVVEA
460 470 480 490 500
AKMANAHDFI MNLPQGYDTE VGERGVKLSG GQKQRLSIAR IFLNNPPILI
510 520 530 540 550
LDEATSALDL ESESIIQEAL DVLSKDRTTL IVAHRLSTIT HADKIVVIEN
560 570
GHIVETGTHR ELIAKQGAYE HLYSIQNL
Length:578
Mass (Da):64,863
Last modified:June 1, 2001 - v1
Checksum:i0DA5945AE8F1799C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58028.1.
RefSeqiWP_000597238.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58028; BAB58028; SAV1866.
KEGGisav:SAV1866.
PATRICi19564578. VBIStaAur52173_1928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58028.1.
RefSeqiWP_000597238.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYDX-ray3.00A/B1-578[»]
2ONJX-ray3.40A/B1-578[»]
4A82electron microscopy2.00A/B/C/D1-578[»]
ProteinModelPortaliQ99T13.
SMRiQ99T13. Positions 1-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60414N.
STRINGi158878.SAV1866.

Proteomic databases

PaxDbiQ99T13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58028; BAB58028; SAV1866.
KEGGisav:SAV1866.
PATRICi19564578. VBIStaAur52173_1928.

Phylogenomic databases

eggNOGiENOG4105BZ1. Bacteria.
COG1132. LUCA.
KOiK11085.
OMAiAISHTNW.
OrthoDBiEOG6T7N3V.
PhylomeDBiQ99T13.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1921-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ99T13.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  2. "Structure of a bacterial multidrug ABC transporter."
    Dawson R.J.P., Locher K.P.
    Nature 443:180-185(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH ADP, FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.

Entry informationi

Entry nameiY1866_STAAM
AccessioniPrimary (citable) accession number: Q99T13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.