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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi374 – 381ATPPROSITE-ProRule annotation8

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:GJJ5-1912-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)DescriptionActionsGraphical viewLength
Topological domaini1 – 15CytoplasmicSequence analysisAdd BLAST15
Transmembranei16 – 36HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini37 – 59ExtracellularSequence analysisAdd BLAST23
Transmembranei60 – 80HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini81 – 138CytoplasmicSequence analysisAdd BLAST58
Transmembranei139 – 159HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini160 – 162ExtracellularSequence analysis3
Transmembranei163 – 183HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini184 – 244CytoplasmicSequence analysisAdd BLAST61
Transmembranei245 – 263HelicalPROSITE-ProRule annotationAdd BLAST19
Topological domaini264 – 269ExtracellularSequence analysis6
Transmembranei270 – 287HelicalPROSITE-ProRule annotationAdd BLAST18
Topological domaini288 – 578CytoplasmicSequence analysisAdd BLAST291

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002715491 – 578Putative multidrug export ATP-binding/permease protein SAV1866Add BLAST578

Proteomic databases

PaxDbiQ99T13.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-60414N.
STRINGi158878.SAV1866.

Structurei

Secondary structure

1578
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 9Combined sources8
Helixi10 – 12Combined sources3
Helixi13 – 24Combined sources12
Turni25 – 27Combined sources3
Helixi28 – 44Combined sources17
Helixi52 – 72Combined sources21
Helixi74 – 106Combined sources33
Helixi109 – 113Combined sources5
Helixi117 – 130Combined sources14
Helixi132 – 136Combined sources5
Helixi137 – 141Combined sources5
Helixi142 – 159Combined sources18
Turni161 – 163Combined sources3
Helixi164 – 167Combined sources4
Helixi170 – 215Combined sources46
Helixi219 – 272Combined sources54
Helixi277 – 285Combined sources9
Helixi287 – 290Combined sources4
Helixi293 – 318Combined sources26
Beta strandi340 – 347Combined sources8
Beta strandi351 – 353Combined sources3
Beta strandi356 – 364Combined sources9
Beta strandi369 – 373Combined sources5
Helixi380 – 384Combined sources5
Turni385 – 389Combined sources5
Beta strandi394 – 400Combined sources7
Helixi405 – 407Combined sources3
Helixi410 – 415Combined sources6
Beta strandi417 – 420Combined sources4
Beta strandi428 – 430Combined sources3
Helixi431 – 435Combined sources5
Helixi436 – 438Combined sources3
Helixi444 – 453Combined sources10
Helixi457 – 461Combined sources5
Helixi466 – 468Combined sources3
Helixi473 – 475Combined sources3
Helixi480 – 494Combined sources15
Beta strandi497 – 503Combined sources7
Turni504 – 507Combined sources4
Helixi510 – 523Combined sources14
Turni524 – 526Combined sources3
Beta strandi527 – 532Combined sources6
Helixi536 – 538Combined sources3
Turni539 – 541Combined sources3
Beta strandi543 – 549Combined sources7
Beta strandi552 – 557Combined sources6
Helixi559 – 564Combined sources6
Helixi568 – 573Combined sources6
Turni574 – 577Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ99T13.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 306ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST291
Domaini340 – 575ABC transporterPROSITE-ProRule annotationAdd BLAST236

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.
OMAiMDFGAIG.
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.
GeneIDi28380492.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HYDX-ray3.00A/B1-578[»]
2ONJX-ray3.40A/B1-578[»]
4A82electron microscopy2.00A/B/C/D1-578[»]
ProteinModelPortaliQ99T13.
SMRiQ99T13.
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.
GeneIDi28380492.
KEGGisav:SAV1866.
PATRICi19564578. VBIStaAur52173_1928.

Phylogenomic databases

eggNOGiENOG4105BZ1. Bacteria.
COG1132. LUCA.
KOiK11085.
OMAiMDFGAIG.
PhylomeDBiQ99T13.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1912-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...

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: November 2, 2016
This is version 109 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.