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P16676 (CYSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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:
Sulfate/thiosulfate import ATP-binding protein CysA

EC=3.6.3.25
Alternative name(s):
Sulfate-transporting ATPase
Gene names
Name:cysA
Ordered Locus Names:b2422, JW2415
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.

Catalytic activity

ATP + H2O + sulfate(Out) = ADP + phosphate + sulfate(In).

Subunit structure

The complex is composed of two ATP-binding proteins (CysA), two transmembrane proteins (CysT and CysW) and a solute-binding protein (CysP) Potential.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity.

Miscellaneous

CysPTWAM system can also transport molybdate.

Sequence similarities

Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family. [View classification]

Contains 1 ABC transporter domain.

Ontologies

Keywords
   Biological processSulfate transport
Transport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentATP-binding cassette (ABC) transporter complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

sulfate transmembrane-transporting ATPase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Sulfate/thiosulfate import ATP-binding protein CysA
PRO_0000092265

Regions

Domain3 – 237235ABC transporter
Nucleotide binding35 – 428ATP Potential

Experimental info

Sequence conflict136 – 1372QL → HV in AAA23639. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16676 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B5FCCA346EDF2788

FASTA36541,059
        10         20         30         40         50         60 
MSIEIANIKK SFGRTQVLND ISLDIPSGQM VALLGPSGSG KTTLLRIIAG LEHQTSGHIR 

        70         80         90        100        110        120 
FHGTDVSRLH ARDRKVGFVF QHYALFRHMT VFDNIAFGLT VLPRRERPNA AAIKAKVTKL 

       130        140        150        160        170        180 
LEMVQLAHLA DRYPAQLSGG QKQRVALARA LAVEPQILLL DEPFGALDAQ VRKELRRWLR 

       190        200        210        220        230        240 
QLHEELKFTS VFVTHDQEEA TEVADRVVVM SQGNIEQADA PDQVWREPAT RFVLEFMGEV 

       250        260        270        280        290        300 
NRLQGTIRGG QFHVGAHRWP LGYTPAYQGP VDLFLRPWEV DISRRTSLDS PLPVQVLEAS 

       310        320        330        340        350        360 
PKGHYTQLVV QPLGWYNEPL TVVMHGDDAP QRGERLFVGL QHARLYNGDE RIETRDEELA 


LAQSA 

« Hide

References

« Hide 'large scale' references
[1]"Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide sequence and expression of the cysTWAM gene cluster."
Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A.
J. Bacteriol. 172:3351-3357(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli."
Rosentel J.K., Healy F., Maupin-Furlow J.A., Lee J.H., Shanmugam K.T.
J. Bacteriol. 177:4857-4864(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE MOLYBDATE TRANSPORT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32101 Genomic DNA. Translation: AAA23639.1.
U00096 Genomic DNA. Translation: AAC75475.1.
AP009048 Genomic DNA. Translation: BAA16296.1.
PIRQRECSA. E65016.
RefSeqNP_416917.1. NC_000913.3.
YP_490658.1. NC_007779.1.

3D structure databases

ProteinModelPortalP16676.
SMRP16676. Positions 1-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9373N.
IntActP16676. 4 interactions.
MINTMINT-1267862.
STRING511145.b2422.

Protein family/group databases

TCDB3.A.1.6.1. the atp-binding cassette (abc) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75475; AAC75475; b2422.
BAA16296; BAA16296; BAA16296.
GeneID12931761.
946889.
KEGGecj:Y75_p2383.
eco:b2422.
PATRIC32120229. VBIEscCol129921_2517.

Organism-specific databases

EchoBASEEB0180.
EcoGeneEG10183. cysA.

Phylogenomic databases

eggNOGCOG1118.
KOK02045.
OMADEMHITS.
OrthoDBEOG6T7N3V.
PhylomeDBP16676.

Enzyme and pathway databases

BioCycEcoCyc:CYSA-MONOMER.
ECOL316407:JW2415-MONOMER.
MetaCyc:CYSA-MONOMER.

Gene expression databases

GenevestigatorP16676.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR014769. ABC_CysA_ATP-bd_C.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR008995. Mo/tungstate-bd_C_term_dom.
IPR027417. P-loop_NTPase.
IPR005666. Sulph_transpt1.
IPR024765. TOBE-like.
[Graphical view]
PfamPF00005. ABC_tran. 1 hit.
PF12857. TOBE_3. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50331. SSF50331. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00968. 3a0106s01. 1 hit.
PROSITEPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS51237. CYSA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP16676.

Entry information

Entry nameCYSA_ECOLI
AccessionPrimary (citable) accession number: P16676
Secondary accession number(s): P77693
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 144 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene