BRXA_BACSU
ID BRXA_BACSU Reviewed; 144 AA.
AC P54170;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bacilliredoxin BrxA {ECO:0000303|PubMed:24313874};
DE Short=Brx-A {ECO:0000303|PubMed:24313874};
DE AltName: Full=Dithiol bacilliredoxin {ECO:0000303|PubMed:24313874};
DE AltName: Full=UPF0403 protein YphP;
GN Name=brxA {ECO:0000303|PubMed:24313874};
GN Synonyms=yphP {ECO:0000303|PubMed:19653655, ECO:0000303|PubMed:24313874};
GN OrderedLocusNames=BSU21860;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 41-61, FUNCTION, INDUCTION, PTM, IDENTIFICATION BY MASS
RP SPECTROMETRY, DISRUPTION PHENOTYPE, MOTIF, ACTIVE SITE, POST-TRANSLATIONAL
RP MODIFICATION AT CYS-53, DISULFIDE BOND, AND MUTAGENESIS OF CYS-53 AND
RP CYS-55.
RX PubMed=24313874; DOI=10.1089/ars.2013.5327;
RA Gaballa A., Chi B.K., Roberts A.A., Becher D., Hamilton C.J., Antelmann H.,
RA Helmann J.D.;
RT "Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and
RT BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and
RT MetE.";
RL Antioxid. Redox Signal. 21:357-367(2014).
RN [4] {ECO:0000312|PDB:3FHK}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF ALA-100/ALA-101 MUTANT, FUNCTION,
RP MOTIF, MUTAGENESIS OF CYS-53 AND CYS-55, AND REACTION MECHANISM OF THE
RP PROTEIN DISULFIDE ISOMERASE ACTIVITY.
RX PubMed=19653655; DOI=10.1021/bi900437z;
RA Derewenda U., Boczek T., Gorres K.L., Yu M., Hung L.W., Cooper D.,
RA Joachimiak A., Raines R.T., Derewenda Z.S.;
RT "Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide
RT isomerase with a CXC catalytic motif.";
RL Biochemistry 48:8664-8671(2009).
CC -!- FUNCTION: S-bacillithiolation is the formation of mixed disulfide bonds
CC between protein thiols and the general thiol reductant bacillithiol
CC (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH)
CC in Firmicutes. This protein is a dithiol bacilliredoxin, which
CC debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB)
CC in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-
CC SSB). Involved in maintaining redox homeostasis in response to
CC disulfide stress conditions (PubMed:24313874). Has a redox potential of
CC -130 mV. Displays weak protein disulfide isomerase activity in vitro
CC (PubMed:19653655). {ECO:0000269|PubMed:19653655,
CC ECO:0000269|PubMed:24313874}.
CC -!- INDUCTION: Expression is up-regulated by cumene hydroperoxide (CHP).
CC {ECO:0000269|PubMed:24313874}.
CC -!- PTM: N-terminal Cys of the CXC active site motif can react with
CC bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation
CC protects Cys residues against overoxidation by acting as a redox switch
CC in response to oxidative stress. {ECO:0000269|PubMed:24313874}.
CC -!- DISRUPTION PHENOTYPE: Mild sensitivity to cumene hydroperoxide (CHP) as
CC indicated by growth inhibition assay. No effect on growth after NaOCl
CC treatment. {ECO:0000269|PubMed:24313874}.
CC -!- SIMILARITY: Belongs to the bacilliredoxin family.
CC {ECO:0000305|PubMed:24313874}.
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DR EMBL; L77246; AAA96630.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14104.1; -; Genomic_DNA.
DR PIR; D69936; D69936.
DR RefSeq; NP_390069.1; NC_000964.3.
DR RefSeq; WP_003230794.1; NZ_JNCM01000036.1.
DR PDB; 3FHK; X-ray; 2.30 A; A/D/E/F=1-144.
DR PDBsum; 3FHK; -.
DR AlphaFoldDB; P54170; -.
DR SMR; P54170; -.
DR STRING; 224308.BSU21860; -.
DR jPOST; P54170; -.
DR PaxDb; P54170; -.
DR PRIDE; P54170; -.
DR EnsemblBacteria; CAB14104; CAB14104; BSU_21860.
DR GeneID; 939085; -.
DR KEGG; bsu:BSU21860; -.
DR PATRIC; fig|224308.179.peg.2388; -.
DR eggNOG; ENOG502ZBVN; Bacteria.
DR OMA; CAAGQCR; -.
DR PhylomeDB; P54170; -.
DR BioCyc; BSUB:BSU21860-MON; -.
DR EvolutionaryTrace; P54170; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR009474; YphP/YqiW.
DR PANTHER; PTHR40052; PTHR40052; 1.
DR Pfam; PF06491; Disulph_isomer; 1.
DR TIGRFAMs; TIGR04191; YphP_YqiW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..144
FT /note="Bacilliredoxin BrxA"
FT /id="PRO_0000049698"
FT MOTIF 53..55
FT /note="CXC active site motif"
FT /evidence="ECO:0000269|PubMed:24313874,
FT ECO:0000305|PubMed:19653655"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24313874"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24313874"
FT MOD_RES 53
FT /note="S-bacillithiol cysteine disulfide"
FT /evidence="ECO:0000269|PubMed:24313874"
FT DISULFID 53..55
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:24313874"
FT MUTAGEN 53
FT /note="C->A: Loss of debacillithiolation of the S-
FT bacillithiolated OhrR (OhrR-SSB) by the NaBH(4)-reduced
FT form of this protein in vitro. Loss of debacillithiolation
FT of in vivo NaOCl-generated S-bacillithiolated MetE (MetE-
FT SSB). Retains isomerization activity of the disulfide bonds
FT in scrambled tachyplesin substrate. Loss of isomerization
FT activity; when associated with A-55."
FT /evidence="ECO:0000269|PubMed:19653655,
FT ECO:0000269|PubMed:24313874"
FT MUTAGEN 55
FT /note="C->A: Accumulation of S-bacillithiolated form due to
FT lack of this resolving cysteine residue.
FT Debacillithiolation of the S-bacillithiolated OhrR (OhrR-
FT SSB) without the prior NaBH(4) reduction of this protein in
FT vitro. Debacillithiolation of in vivo NaOCl-generated S-
FT bacillithiolated MetE (MetE-SSB). Retains isomerization
FT activity of the disulfide bonds in scrambled tachyplesin
FT substrate. Loss of isomerization activity; when associated
FT with A-53."
FT /evidence="ECO:0000269|PubMed:19653655,
FT ECO:0000269|PubMed:24313874"
FT HELIX 1..21
FT /evidence="ECO:0007829|PDB:3FHK"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:3FHK"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:3FHK"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3FHK"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:3FHK"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3FHK"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3FHK"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3FHK"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:3FHK"
SQ SEQUENCE 144 AA; 15875 MW; D3CAF2EBCC41078C CRC64;
MSMAYEEYMR QLVVPMRREL TGAGFEELTT AEEVENFMEK AEGTTLVVVN SVCGCAAGLA
RPAATQAVLQ NDKTPDNTVT VFAGQDKEAT AKMREYFTGQ EPSSPSMALL KGKEVVHFIP
RHEIEGHDME EIMKNLTAAF DAHC
