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Protein
Submitted name:

Mn transporter MntC

Gene

mntC

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

Functioni

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. metal ion transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

TransportUniRule annotation

Keywords - Ligandi

ManganeseCombined sources, Metal-bindingCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Mn transporter MntCImported
Gene namesi
Name:mntCImported
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)Imported
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

Interactioni

Protein-protein interaction databases

IntActiQ79EF9. 1 interaction.
STRINGi1148.sll1598.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVLX-ray2.90A/B/C26-330[»]
3UJPX-ray2.70A/B/C24-330[»]
4IRMX-ray3.50A/B/C1-330[»]
ProteinModelPortaliQ79EF9.
SMRiQ79EF9. Positions 49-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ79EF9.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial solute-binding protein 9 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0803.
HOGENOMiHOG000180310.
InParanoidiQ79EF9.
KOiK11601.
OMAiTEGKEDP.
PhylomeDBiQ79EF9.

Family and domain databases

InterProiIPR006129. AdhesinB.
IPR006128. Lipoprotein_4.
IPR006127. Perip_solute-bd_prot_fam.
[Graphical view]
PANTHERiPTHR30477:SF1. PTHR30477:SF1. 1 hit.
PfamiPF01297. TroA. 1 hit.
[Graphical view]
PRINTSiPR00691. ADHESINB.
PR00690. ADHESNFAMILY.

Sequencei

Sequence statusi: Complete.

Q79EF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSFASRGG LLASGLAIAF WLTGCGTAEV TTSNAPSEEV TAVTTEVQGE
60 70 80 90 100
TEEKKKVLTT FTVLADMVQN VAGDKLVVES ITRIGAEIHG YEPTPSDIVK
110 120 130 140 150
AQDADLILYN GMNLERWFEQ FLGNVKDVPS VVLTEGIEPI PIADGPYTDK
160 170 180 190 200
PNPHAWMSPR NALVYVENIR QAFVELDPDN AKYYNANAAV YSEQLKAIDR
210 220 230 240 250
QLGADLEQVP ANQRFLVSCE GAFSYLARDY GMEEIYMWPI NAEQQFTPKQ
260 270 280 290 300
VQTVIEEVKT NNVPTIFCES TVSDKGQKQV AQATGARFGG NLYVDSLSTE
310 320 330
EGPVPTFLDL LEYDARVITN GLLAGTNAQQ
Length:330
Mass (Da):36,075
Last modified:July 5, 2004 - v1
Checksum:iFE9F510020719D80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17919.1.
RefSeqiNP_441239.1. NC_000911.1.
YP_005651296.1. NC_017277.1.
YP_007451121.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA17919; BAA17919; BAA17919.
GeneIDi954581.
KEGGisyn:sll1598.
PATRICi23839820. VBISynSp132158_1471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17919.1.
RefSeqiNP_441239.1. NC_000911.1.
YP_005651296.1. NC_017277.1.
YP_007451121.1. NC_020286.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVLX-ray2.90A/B/C26-330[»]
3UJPX-ray2.70A/B/C24-330[»]
4IRMX-ray3.50A/B/C1-330[»]
ProteinModelPortaliQ79EF9.
SMRiQ79EF9. Positions 49-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ79EF9. 1 interaction.
STRINGi1148.sll1598.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17919; BAA17919; BAA17919.
GeneIDi954581.
KEGGisyn:sll1598.
PATRICi23839820. VBISynSp132158_1471.

Phylogenomic databases

eggNOGiCOG0803.
HOGENOMiHOG000180310.
InParanoidiQ79EF9.
KOiK11601.
OMAiTEGKEDP.
PhylomeDBiQ79EF9.

Miscellaneous databases

EvolutionaryTraceiQ79EF9.

Family and domain databases

InterProiIPR006129. AdhesinB.
IPR006128. Lipoprotein_4.
IPR006127. Perip_solute-bd_prot_fam.
[Graphical view]
PANTHERiPTHR30477:SF1. PTHR30477:SF1. 1 hit.
PfamiPF01297. TroA. 1 hit.
[Graphical view]
PRINTSiPR00691. ADHESINB.
PR00690. ADHESNFAMILY.
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. "The MntC crystal structure suggests that import of Mn2+ in cyanobacteria is redox controlled."
    Rukhman V., Anati R., Melamed-Frank M., Adir N.
    J. Mol. Biol. 348:961-969(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-330 IN COMPLEX WITH MANGANESE, ACTIVE SITE.
  3. "Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein."
    Kanteev M., Adir N.
    Acta Crystallogr. F 69:237-242(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-330 IN COMPLEX WITH MANGANESE AND ZINC, ACTIVE SITE.

Entry informationi

Entry nameiQ79EF9_SYNY3
AccessioniPrimary (citable) accession number: Q79EF9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 88 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.