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 03-AUG-2022, entry version 151.
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; DOI=10.1128/jb.180.7.1655-1661.1998;
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:0007744|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:0007744|PDB:1Z2D, ECO:0007744|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:0007744|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}.
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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 AlphaFoldDB; P45947; -.
DR BMRB; P45947; -.
DR SMR; P45947; -.
DR STRING; 224308.BSU25780; -.
DR PaxDb; P45947; -.
DR PRIDE; P45947; -.
DR EnsemblBacteria; CAB14519; CAB14519; BSU_25780.
DR GeneID; 937801; -.
DR KEGG; bsu:BSU25780; -.
DR PATRIC; fig|224308.179.peg.2802; -.
DR eggNOG; COG0394; Bacteria.
DR InParanoid; P45947; -.
DR OMA; DNAKERC; -.
DR PhylomeDB; P45947; -.
DR BioCyc; BSUB:BSU25780-MON; -.
DR BRENDA; 1.20.4.4; 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;
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:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:16192272, ECO:0007744|PDB:1Z2E"
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:0007829|PDB:1JL3"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1JL3"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1Z2E"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1JL3"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1JL3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1Z2D"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1JL3"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1JL3"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1JL3"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1JL3"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1JL3"
FT HELIX 113..137
FT /evidence="ECO:0007829|PDB:1JL3"
SQ SEQUENCE 139 AA; 15595 MW; 880EE1C77D1FE130 CRC64;
MENKIIYFLC TGNSCRSQMA EGWAKQYLGD EWKVYSAGIE AHGLNPNAVK AMKEVGIDIS
NQTSDIIDSD ILNNADLVVT LCGDAADKCP MTPPHVKREH WGFDDPARAQ GTEEEKWAFF
QRVRDEIGNR LKEFAETGK
