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Protein
Submitted name:

Ssr2857 protein

Gene

ssr2857

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121CopperCombined sources
Metal bindingi15 – 151CopperCombined sources

GO - Molecular functioni

  • copper ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

CopperCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Ssr2857 proteinImported
Gene namesi
Ordered Locus Names:ssr2857Imported
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)Imported
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PaxDbiP73213.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
slr1950P745123EBI-904975,EBI-905009

Protein-protein interaction databases

DIPiDIP-35106N.
IntActiP73213. 2 interactions.
MINTiMINT-223899.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SB6NMR-A1-64[»]
2XMJX-ray1.08A/B1-64[»]
2XMKX-ray1.35A/B1-64[»]
2XMMX-ray1.65A/B1-60[»]
A/B62-64[»]
2XMTX-ray1.50A/B1-64[»]
2XMUX-ray1.75A/B1-64[»]
2XMVX-ray1.80A/B/C/D/E/F1-64[»]
4A46X-ray1.85A/B/C/D2-64[»]
4A47X-ray1.90A/B/C/D2-64[»]
ProteinModelPortaliP73213.
SMRiP73213. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP73213.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2608.
HOGENOMiHOG000038877.
InParanoidiP73213.
KOiK07213.
OMAiTVPKLAC.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P73213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIQLTVPTI ACEACAEAVT KAVQNEDAQA TVQVDLTSKK VTITSALGEE
60
QLRTAIASAG HEVE
Length:64
Mass (Da):6,686
Last modified:February 1, 1997 - v1
Checksum:i111676DBB03D032E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17240.1.
PIRiS75326.

Genome annotation databases

EnsemblBacteriaiBAA17240; BAA17240; BAA17240.
KEGGisyy:SYNGTS_0665.
syz:MYO_16710.
PATRICi23838306. VBISynSp132158_0720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17240.1.
PIRiS75326.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SB6NMR-A1-64[»]
2XMJX-ray1.08A/B1-64[»]
2XMKX-ray1.35A/B1-64[»]
2XMMX-ray1.65A/B1-60[»]
A/B62-64[»]
2XMTX-ray1.50A/B1-64[»]
2XMUX-ray1.75A/B1-64[»]
2XMVX-ray1.80A/B/C/D/E/F1-64[»]
4A46X-ray1.85A/B/C/D2-64[»]
4A47X-ray1.90A/B/C/D2-64[»]
ProteinModelPortaliP73213.
SMRiP73213. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35106N.
IntActiP73213. 2 interactions.
MINTiMINT-223899.

Proteomic databases

PaxDbiP73213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17240; BAA17240; BAA17240.
KEGGisyy:SYNGTS_0665.
syz:MYO_16710.
PATRICi23838306. VBISynSp132158_0720.

Phylogenomic databases

eggNOGiCOG2608.
HOGENOMiHOG000038877.
InParanoidiP73213.
KOiK07213.
OMAiTVPKLAC.

Miscellaneous databases

EvolutionaryTraceiP73213.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / KazusaImported.
  2. "Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif."
    Banci L., Bertini I., Ciofi-Baffoni S., Su X.C., Borrelly G.P., Robinson N.J.
    J. Biol. Chem. 279:27502-27510(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  3. "Visualizing the metal-binding versatility of copper trafficking sites ."
    Badarau A., Firbank S.J., McCarthy A.A., Banfield M.J., Dennison C.
    Biochemistry 49:7798-7810(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) IN COMPLEX WITH COPPER.
  4. "Investigating the role of zinc and copper binding motifs of trafficking sites in the cyanobacterium Synechocystis PCC 6803."
    Badarau A., Basle A., Firbank S.J., Dennison C.
    Biochemistry 52:6816-6823(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-64.
  5. "Crosstalk between Cu(I) and Zn(II) homeostasis via Atx1 and cognate domains."
    Badarau A., Basle A., Firbank S.J., Dennison C.
    Chem. Commun. (Camb.) 49:8000-8002(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-64.

Entry informationi

Entry nameiP73213_SYNY3
AccessioniPrimary (citable) accession number: P73213
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: July 22, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.