Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

High-affinity zinc uptake system binding-protein ZnuA

Gene

znuA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Part of the high-affinity ABC transporter complex ZnuABC involved in zinc import (Probable). ZnuABC-mediated zinc transport is required for comF expression and competence development.Curated2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport, Zinc transport

Keywords - Ligandi

Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU02850-MONOMER.

Protein family/group databases

TCDBi3.A.1.15.11. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
High-affinity zinc uptake system binding-protein ZnuA
Gene namesi
Name:znuA
Synonyms:adcA, ycdH
Ordered Locus Names:BSU02850
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow slowly in zinc-deficient medium; this effect is suppressed upon addition of exogenous Zn2+. Growth is slower yet in a double knockout with YciC. Disruption results in low transformability.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020PROSITE-ProRule annotationAdd
BLAST
Chaini21 – 319299High-affinity zinc uptake system binding-protein ZnuAPRO_0000360809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi21 – 211S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiO34966.

Expressioni

Inductioni

Repressed by zinc via the metallo-regulatory protein Zur.2 Publications

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).Curated

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001573.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Helixi44 – 5411Combined sources
Helixi55 – 573Combined sources
Beta strandi58 – 647Combined sources
Turni70 – 723Combined sources
Helixi77 – 859Combined sources
Beta strandi86 – 927Combined sources
Turni94 – 963Combined sources
Helixi100 – 1056Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi113 – 1164Combined sources
Turni117 – 1204Combined sources
Helixi149 – 1513Combined sources
Helixi153 – 17018Combined sources
Helixi172 – 1743Combined sources
Helixi175 – 20127Combined sources
Beta strandi207 – 2126Combined sources
Helixi216 – 2216Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi234 – 2363Combined sources
Helixi240 – 24910Combined sources
Beta strandi257 – 2593Combined sources
Helixi266 – 2749Combined sources
Beta strandi279 – 2813Combined sources
Helixi291 – 2966Combined sources
Helixi300 – 31516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O1EX-ray2.60A/B22-319[»]
ProteinModelPortaliO34966.
SMRiO34966. Positions 36-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34966.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105DSE. Bacteria.
COG0803. LUCA.
HOGENOMiHOG000180308.
InParanoidiO34966.
KOiK09815.
OMAiIYHPALS.
OrthoDBiEOG6K9QKM.
PhylomeDBiO34966.

Family and domain databases

InterProiIPR006129. AdhesinB.
IPR006128. Lipoprotein_4.
IPR006127. ZnuA-like.
[Graphical view]
PfamiPF01297. ZnuA. 1 hit.
[Graphical view]
PRINTSiPR00691. ADHESINB.
PR00690. ADHESNFAMILY.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKWSGLFV IAACFLLVAA CGNSSTKGSA DSKGDKLHVV TTFYPMYEFT
60 70 80 90 100
KQIVKDKGDV DLLIPSSVEP HDWEPTPKDI ANIQDADLFV YNSEYMETWV
110 120 130 140 150
PSAEKSMGQG HAVFVNASKG IDLMEGSEEE HEEHDHGEHE HSHAMDPHVW
160 170 180 190 200
LSPVLAQKEV KNITAQIVKQ DPDNKEYYEK NSKEYIAKLQ DLDKLYRTTA
210 220 230 240 250
KKAEKKEFIT QHTAFGYLAK EYGLKQVPIA GLSPDQEPSA ASLAKLKTYA
260 270 280 290 300
KEHNVKVIYF EEIASSKVAD TLASEIGAKT EVLNTLEGLS KEEQDKGLGY
310
IDIMKQNLDA LKDSLLVKS
Length:319
Mass (Da):35,660
Last modified:January 1, 1998 - v1
Checksum:iC66128D4FDE94D1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000617 Genomic DNA. Translation: BAA22246.1.
AL009126 Genomic DNA. Translation: CAB12079.1.
PIRiA69756.
RefSeqiNP_388167.1. NC_000964.3.
WP_003234733.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB12079; CAB12079; BSU02850.
GeneIDi938370.
KEGGibsu:BSU02850.
PATRICi18972129. VBIBacSub10457_0293.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000617 Genomic DNA. Translation: BAA22246.1.
AL009126 Genomic DNA. Translation: CAB12079.1.
PIRiA69756.
RefSeqiNP_388167.1. NC_000964.3.
WP_003234733.1. NZ_JNCM01000030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O1EX-ray2.60A/B22-319[»]
ProteinModelPortaliO34966.
SMRiO34966. Positions 36-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001573.

Protein family/group databases

TCDBi3.A.1.15.11. the atp-binding cassette (abc) superfamily.

Proteomic databases

PaxDbiO34966.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12079; CAB12079; BSU02850.
GeneIDi938370.
KEGGibsu:BSU02850.
PATRICi18972129. VBIBacSub10457_0293.

Phylogenomic databases

eggNOGiENOG4105DSE. Bacteria.
COG0803. LUCA.
HOGENOMiHOG000180308.
InParanoidiO34966.
KOiK09815.
OMAiIYHPALS.
OrthoDBiEOG6K9QKM.
PhylomeDBiO34966.

Enzyme and pathway databases

BioCyciBSUB:BSU02850-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34966.

Family and domain databases

InterProiIPR006129. AdhesinB.
IPR006128. Lipoprotein_4.
IPR006127. ZnuA-like.
[Graphical view]
PfamiPF01297. ZnuA. 1 hit.
[Graphical view]
PRINTSiPR00691. ADHESINB.
PR00690. ADHESNFAMILY.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation."
    Kumano M., Tamakoshi A., Yamane K.
    Microbiology 143:2775-2782(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis."
    Gaballa A., Helmann J.D.
    J. Bacteriol. 180:5815-5821(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
  4. "Functional analysis of the Bacillus subtilis Zur regulon."
    Gaballa A., Wang T., Ye R.W., Helmann J.D.
    J. Bacteriol. 184:6508-6514(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168.
  5. "Profiling and comprehensive expression analysis of ABC transporter solute-binding proteins of Bacillus subtilis membrane based on a proteomic approach."
    Bunai K., Ariga M., Inoue T., Nozaki M., Ogane S., Kakeshita H., Nemoto T., Nakanishi H., Yamane K.
    Electrophoresis 25:141-155(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "ZnuABC and ZosA zinc transporters are differently involved in competence development in Bacillus subtilis."
    Ogura M.
    J. Biochem. 150:615-625(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COMPETENCE DEVELOPMENT, DISRUPTION PHENOTYPE, GENE NAME.
    Strain: 168.
  7. "Crystal structure of the metal-dependent lipoprotein YcdH from Bacillus subtilis, northeast structural genomics target sr583."
    Northeast structural genomics consortium (NESG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 22-319.

Entry informationi

Entry nameiZNUA_BACSU
AccessioniPrimary (citable) accession number: O34966
Secondary accession number(s): Q797R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 99 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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.