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Protein

HTH-type transcriptional repressor CzrA

Gene

czrA

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

Functioni

Metal-responsive transcriptional regulator that represses transcription of cadA and the czcD-trkA operon by binding specifically to their promoter. Binding of zinc causes the repressor to dissociate from the DNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901ZincPROSITE-ProRule annotation
Metal bindingi92 – 921ZincPROSITE-ProRule annotation
Metal bindingi103 – 1031ZincPROSITE-ProRule annotation
Metal bindingi106 – 1061ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi48 – 7124H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU19120-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional repressor CzrA
Gene namesi
Name:czrA
Synonyms:yozA
Ordered Locus Names:BSU19120
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107HTH-type transcriptional repressor CzrAPRO_0000378472Add
BLAST

Proteomic databases

PaxDbiO31844.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010556.

Structurei

3D structure databases

ProteinModelPortaliO31844.
SMRiO31844. Positions 12-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 10794HTH arsR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH arsR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105KTU. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiO31844.
OMAiMIHHTRH.
OrthoDBiEOG6Z3KS4.
PhylomeDBiO31844.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50987. HTH_ARSR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFRETEQS AADLDEETLF LVAQTFKALS DPTRIRILHL LSQGEHAVNG
60 70 80 90 100
IAEKLNLLQS TVSHQLRFLK NLRLVKSRRE GTSIYYSPED EHVLDVLQQM

IHHTQHD
Length:107
Mass (Da):12,379
Last modified:January 1, 1998 - v1
Checksum:i1F5D693B9DBF0ABB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13804.1.
PIRiE69930.
RefSeqiNP_389793.1. NC_000964.3.
WP_003231284.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB13804; CAB13804; BSU19120.
GeneIDi939658.
KEGGibsu:BSU19120.
PATRICi18975671. VBIBacSub10457_2026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13804.1.
PIRiE69930.
RefSeqiNP_389793.1. NC_000964.3.
WP_003231284.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliO31844.
SMRiO31844. Positions 12-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010556.

Proteomic databases

PaxDbiO31844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13804; CAB13804; BSU19120.
GeneIDi939658.
KEGGibsu:BSU19120.
PATRICi18975671. VBIBacSub10457_2026.

Phylogenomic databases

eggNOGiENOG4105KTU. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiO31844.
OMAiMIHHTRH.
OrthoDBiEOG6Z3KS4.
PhylomeDBiO31844.

Enzyme and pathway databases

BioCyciBSUB:BSU19120-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50987. HTH_ARSR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "Predicting metals sensed by ArsR-SmtB repressors: allosteric interference by a non-effector metal."
    Harvie D.R., Andreini C., Cavallaro G., Meng W., Connolly B.A., Yoshida K., Fujita Y., Harwood C.R., Radford D.S., Tottey S., Cavet J.S., Robinson N.J.
    Mol. Microbiol. 59:1341-1356(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
    Strain: 168.

Entry informationi

Entry nameiCZRA_BACSU
AccessioniPrimary (citable) accession number: O31844
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Can bind copper. It does not affect DNA binding but it inhibits zinc-mediated regulation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.