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Protein

Probable pyridine nucleotide-disulfide oxidoreductase RclA

Gene

rclA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probably involved in reactive chlorine species (RCS) stress resistance.1 Publication

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei426 – 4261Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 4311FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • response to hypochlorite Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:G6174-MONOMER.
ECOL316407:JW5040-MONOMER.
RETL1328306-WGS:GSTH-6131-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable pyridine nucleotide-disulfide oxidoreductase RclA
Alternative name(s):
Reactive chlorine resistance protein A
Gene namesi
Name:rclA
Synonyms:ykgC
Ordered Locus Names:b0304, JW5040
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13580. rclA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutants are more sensitive to HOCl treatment than wild-type cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Probable pyridine nucleotide-disulfide oxidoreductase RclAPRO_0000068059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 48Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP77212.
PRIDEiP77212.

Expressioni

Inductioni

Induced by RclR in response to hypochlorous acid (HOCl).1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4259800. 10 interactions.
DIPiDIP-12675N.
IntActiP77212. 2 interactions.
MINTiMINT-1306527.
STRINGi511145.b0304.

Structurei

3D structure databases

ProteinModelPortaliP77212.
SMRiP77212. Positions 2-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276709.
InParanoidiP77212.
OMAiCTPTKTM.
OrthoDBiEOG6QCD6D.
PhylomeDBiP77212.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77212-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP
60 70 80 90 100
TKTLVHDAQQ HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVIDGQAE
110 120 130 140 150
FINNHSLRVH RPEGNLEIHG EKIFINTGAQ TVVPPIPGIT TTPGVYDSTG
160 170 180 190 200
LLNLKELPGH LGILGGGYIG VEFASMFANF GSKVTILEAA SLFLPREDRD
210 220 230 240 250
IADNIATILR DQGVDIILNA HVERISHHEN QVQVHSEHAQ LAVDALLIAS
260 270 280 290 300
GRQPATASLH PENAGIAVNE RGAIVVDKRL HTTADNIWAM GDVTGGLQFT
310 320 330 340 350
YISLDDYRIV RDELLGEGKR STDDRKNVPY SVFMTPPLSR VGMTEEQARE
360 370 380 390 400
SGADIQVVTL PVAAIPRARV MNDTRGVLKA IVDNKTQRML GASLLCVDSH
410 420 430 440
EMINIVKMVM DAGLPYSILR DQIFTHPSMS ESLNDLFSLV K
Length:441
Mass (Da):48,244
Last modified:August 29, 2001 - v2
Checksum:i53B9C0B52C7DA8A0
GO

Sequence cautioni

The sequence AAB18031.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73857 Genomic DNA. Translation: AAB18031.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73407.2.
AP009048 Genomic DNA. Translation: BAE76088.1.
PIRiH64756.
RefSeqiNP_414838.2. NC_000913.3.
WP_001046307.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73407; AAC73407; b0304.
BAE76088; BAE76088; BAE76088.
GeneIDi946092.
KEGGiecj:JW5040.
eco:b0304.
PATRICi32115737. VBIEscCol129921_0311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73857 Genomic DNA. Translation: AAB18031.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73407.2.
AP009048 Genomic DNA. Translation: BAE76088.1.
PIRiH64756.
RefSeqiNP_414838.2. NC_000913.3.
WP_001046307.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP77212.
SMRiP77212. Positions 2-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259800. 10 interactions.
DIPiDIP-12675N.
IntActiP77212. 2 interactions.
MINTiMINT-1306527.
STRINGi511145.b0304.

Proteomic databases

PaxDbiP77212.
PRIDEiP77212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73407; AAC73407; b0304.
BAE76088; BAE76088; BAE76088.
GeneIDi946092.
KEGGiecj:JW5040.
eco:b0304.
PATRICi32115737. VBIEscCol129921_0311.

Organism-specific databases

EchoBASEiEB3350.
EcoGeneiEG13580. rclA.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276709.
InParanoidiP77212.
OMAiCTPTKTM.
OrthoDBiEOG6QCD6D.
PhylomeDBiP77212.

Enzyme and pathway databases

BioCyciEcoCyc:G6174-MONOMER.
ECOL316407:JW5040-MONOMER.
RETL1328306-WGS:GSTH-6131-MONOMER.

Miscellaneous databases

PROiP77212.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli."
    Parker B.W., Schwessinger E.A., Jakob U., Gray M.J.
    J. Biol. Chem. 288:32574-32584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, GENE NAME.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiRCLA_ECOLI
AccessioniPrimary (citable) accession number: P77212
Secondary accession number(s): Q2MCB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 29, 2001
Last modified: January 20, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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