(data stored in SCRATCH zone)

SWISSPROT: ARSC_BACSU

ID   ARSC_BACSU              Reviewed;         139 AA.
AC   P45947;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 141.
DE   RecName: Full=Arsenate reductase {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000303|PubMed:9537360};
DE            EC=1.20.4.4 {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000269|PubMed:16797027};
DE   AltName: Full=Arsenical pump modifier;
DE   AltName: Full=Protein ArsC;
GN   Name=arsC {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000303|PubMed:7704261};
GN   Synonyms=yqcM; OrderedLocusNames=BSU25780;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=7704261; DOI=10.1099/13500872-141-2-323;
RA   Takemaru K., Mizuno M., Sato T., Takeuchi M., Kobayashi Y.;
RT   "Complete nucleotide sequence of a skin element excised by DNA
RT   rearrangement during sporulation in Bacillus subtilis.";
RL   Microbiology 141:323-327(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=7489895; DOI=10.1016/0378-1119(95)00636-k;
RA   Medigue C., Moszer I., Viari A., Danchin A.;
RT   "Analysis of a Bacillus subtilis genome fragment using a co-operative
RT   computer system prototype.";
RL   Gene 165:GC37-GC51(1995).
RN   [5]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / JH642;
RX   PubMed=9537360;
RA   Sato T., Kobayashi Y.;
RT   "The ars operon in the skin element of Bacillus subtilis confers resistance
RT   to arsenate and arsenite.";
RL   J. Bacteriol. 180:1655-1661(1998).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF LYS-33.
RX   PubMed=16797027; DOI=10.1016/j.jmb.2006.05.054;
RA   Roos G., Buts L., Van Belle K., Brosens E., Geerlings P., Loris R.,
RA   Wyns L., Messens J.;
RT   "Interplay between ion binding and catalysis in the thioredoxin-coupled
RT   arsenate reductase family.";
RL   J. Mol. Biol. 360:826-838(2006).
RN   [7] {ECO:0000244|PDB:1JL3}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=11698660; DOI=10.1073/pnas.241397198;
RA   Bennett M.S., Guan Z., Laurberg M., Su X.D.;
RT   "Bacillus subtilis arsenate reductase is structurally and functionally
RT   similar to low molecular weight protein tyrosine phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:13577-13582(2001).
RN   [8] {ECO:0000244|PDB:1Z2D, ECO:0000244|PDB:1Z2E}
RP   STRUCTURE BY NMR OF REDUCED AND OXIDIZED FORMS, AND REACTION MECHANISM.
RX   PubMed=16192272; DOI=10.1074/jbc.m508132200;
RA   Guo X., Li Y., Peng K., Hu Y., Li C., Xia B., Jin C.;
RT   "Solution structures and backbone dynamics of arsenate reductase from
RT   Bacillus subtilis: reversible conformational switch associated with
RT   arsenate reduction.";
RL   J. Biol. Chem. 280:39601-39608(2005).
RN   [9] {ECO:0000244|PDB:2IPA}
RP   STRUCTURE BY NMR IN COMPLEX WITH THIOREDOXIN.
RX   PubMed=17303556; DOI=10.1074/jbc.m700970200;
RA   Li Y., Hu Y., Zhang X., Xu H., Lescop E., Xia B., Jin C.;
RT   "Conformational fluctuations coupled to the thiol-disulfide transfer
RT   between thioredoxin and arsenate reductase in Bacillus subtilis.";
RL   J. Biol. Chem. 282:11078-11083(2007).
CC   -!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
CC       [As(III)] (PubMed:16797027). In vitro, can dephosphorylate para-
CC       nitrophenyl phosphate (pNPP) (PubMed:11698660).
CC       {ECO:0000269|PubMed:11698660, ECO:0000269|PubMed:16797027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-
CC         disulfide + arsenite + H2O; Xref=Rhea:RHEA:43848, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:48597, ChEBI:CHEBI:50058; EC=1.20.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01624,
CC         ECO:0000269|PubMed:16797027};
CC   -!- ACTIVITY REGULATION: Activity is potassium and sulfate-independent.
CC       {ECO:0000269|PubMed:16797027}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54 uM for arsenate (in the presence of KCl)
CC         {ECO:0000269|PubMed:16797027};
CC         KM=58 uM for arsenate (in the presence of NaCl)
CC         {ECO:0000269|PubMed:16797027};
CC         KM=64 uM for arsenate (in the presence of Na(2)SO(4))
CC         {ECO:0000269|PubMed:16797027};
CC         KM=47 uM for arsenate (in the presence of K(2)SO(4))
CC         {ECO:0000269|PubMed:16797027};
CC         Note=kcat is 96 min(-1) in the presence of KCl (PubMed:16797027).
CC         kcat is 80 min(-1) in the presence of NaCl (PubMed:16797027). kcat is
CC         120 min(-1) in the presence of Na(2)SO(4) (PubMed:16797027). kcat is
CC         95 min(-1) in the presence of K(2)SO(4) (PubMed:16797027).
CC         {ECO:0000269|PubMed:16797027};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11698660}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624}.
CC   -!- INDUCTION: Induced by arsenate, arsenite, and antimonite.
CC       {ECO:0000269|PubMed:9537360}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is sensitive to arsenate but is still
CC       resistant to arsenite. {ECO:0000269|PubMed:9537360}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. Thioredoxin-coupled ArsC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000305}.
DR   EMBL; D32216; BAA06970.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12434.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14519.1; -; Genomic_DNA.
DR   PIR; C69950; C69950.
DR   RefSeq; NP_390455.1; NC_000964.3.
DR   RefSeq; WP_004398596.1; NZ_JNCM01000036.1.
DR   PDB; 1JL3; X-ray; 1.60 A; A/B/C/D=1-139.
DR   PDB; 1Z2D; NMR; -; A=1-139.
DR   PDB; 1Z2E; NMR; -; A=1-139.
DR   PDB; 2IPA; NMR; -; B=1-139.
DR   PDBsum; 1JL3; -.
DR   PDBsum; 1Z2D; -.
DR   PDBsum; 1Z2E; -.
DR   PDBsum; 2IPA; -.
DR   SMR; P45947; -.
DR   STRING; 224308.BSU25780; -.
DR   PaxDb; P45947; -.
DR   PRIDE; P45947; -.
DR   EnsemblBacteria; CAB14519; CAB14519; BSU25780.
DR   GeneID; 937801; -.
DR   KEGG; bsu:BSU25780; -.
DR   PATRIC; fig|224308.179.peg.2802; -.
DR   eggNOG; ENOG4108UXE; Bacteria.
DR   eggNOG; COG0394; LUCA.
DR   HOGENOM; HOG000273093; -.
DR   InParanoid; P45947; -.
DR   KO; K03741; -.
DR   OMA; ACPVYFG; -.
DR   PhylomeDB; P45947; -.
DR   BioCyc; BSUB:BSU25780-MONOMER; -.
DR   BRENDA; 1.20.4.B2; 658.
DR   SABIO-RK; P45947; -.
DR   EvolutionaryTrace; P45947; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   HAMAP; MF_01624; Arsenate_reduct; 1.
DR   InterPro; IPR014064; Arsenate_reductase_ArsC.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
DR   TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P45947.
DR   SWISS-2DPAGE; P45947.
KW   3D-structure; Arsenical resistance; Cytoplasm; Disulfide bond;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..139
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162520"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT                   ECO:0000305|PubMed:11698660"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT                   ECO:0000305|PubMed:11698660"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT                   ECO:0000305|PubMed:11698660"
FT   DISULFID        10..82
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT                   ECO:0000305|PubMed:16192272"
FT   DISULFID        82..89
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000244|PDB:1Z2E, ECO:0000255|HAMAP-
FT                   Rule:MF_01624, ECO:0000305|PubMed:16192272"
FT   MUTAGEN         33
FT                   /note="K->N: Binds potassium in the micromolar range."
FT                   /evidence="ECO:0000269|PubMed:16797027"
FT   STRAND          4..15
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           16..27
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   TURN            28..30
FT                   /evidence="ECO:0000244|PDB:1Z2E"
FT   STRAND          32..40
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           46..54
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           59..61
FT                   /evidence="ECO:0000244|PDB:1Z2D"
FT   HELIX           69..72
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   STRAND          76..80
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           83..88
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   STRAND          96..100
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           106..108
FT                   /evidence="ECO:0000244|PDB:1JL3"
FT   HELIX           113..137
FT                   /evidence="ECO:0000244|PDB:1JL3"
SQ   SEQUENCE   139 AA;  15595 MW;  880EE1C77D1FE130 CRC64;
     MENKIIYFLC TGNSCRSQMA EGWAKQYLGD EWKVYSAGIE AHGLNPNAVK AMKEVGIDIS
     NQTSDIIDSD ILNNADLVVT LCGDAADKCP MTPPHVKREH WGFDDPARAQ GTEEEKWAFF
     QRVRDEIGNR LKEFAETGK
//

If you have problems or comments...

PBIL Back to PBIL home page