SPX_STAA8
ID SPX_STAA8 Reviewed; 131 AA.
AC Q2G1U6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Global transcriptional regulator Spx {ECO:0000255|HAMAP-Rule:MF_01132};
GN Name=spx {ECO:0000255|HAMAP-Rule:MF_01132, ECO:0000303|PubMed:16788195};
GN OrderedLocusNames=SAOUHSC_00934 {ECO:0000312|EMBL:ABD30059.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8325-4;
RX PubMed=16788195; DOI=10.1128/jb.00194-06;
RA Pamp S.J., Frees D., Engelmann S., Hecker M., Ingmer H.;
RT "Spx is a global effector impacting stress tolerance and biofilm formation
RT in Staphylococcus aureus.";
RL J. Bacteriol. 188:4861-4870(2006).
RN [3]
RP FUNCTION.
RC STRAIN=8325-4;
RX PubMed=23629700; DOI=10.1128/aac.00220-13;
RA Jousselin A., Kelley W.L., Barras C., Lew D.P., Renzoni A.;
RT "The Staphylococcus aureus thiol/oxidative stress global regulator Spx
RT controls trfA, a gene implicated in cell wall antibiotic resistance.";
RL Antimicrob. Agents Chemother. 57:3283-3292(2013).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=HG003;
RX PubMed=32117138; DOI=10.3389/fmicb.2020.00113;
RA Panasenko O.O., Bezrukov F., Komarynets O., Renzoni A.;
RT "YjbH solubility controls Spx in Staphylococcus aureus: implication for
RT MazEF toxin-antitoxin system regulation.";
RL Front. Microbiol. 11:113-113(2020).
CC -!- FUNCTION: Global transcriptional regulator that plays a key role in
CC stress response and exerts either positive or negative regulation of
CC genes (PubMed:16788195). Acts by interacting with the C-terminal domain
CC of the alpha subunit of the RNA polymerase (RNAP) (By similarity). This
CC interaction can enhance binding of RNAP to the promoter region of
CC target genes and stimulate their transcription, or block interaction of
CC RNAP with activator proteins and repress transcription (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01132, ECO:0000269|PubMed:16788195}.
CC -!- FUNCTION: Required for transcription of thioredoxin reductase (trxB).
CC Modulates the expression of icaR, encoding a repressor of the biofilm
CC operon icaADBC (PubMed:16788195). Also controls the transcription of
CC trfA, a gene implicated in cell wall antibiotic resistance, which in
CC turn is required for degradation of MazE antitoxin, the unstable
CC component of the MazEF toxin-antitoxin system, that neutralizes the
CC endoribonuclease activity of MazF toxin (PubMed:23629700,
CC PubMed:32117138). {ECO:0000269|PubMed:16788195,
CC ECO:0000269|PubMed:23629700, ECO:0000269|PubMed:32117138}.
CC -!- ACTIVITY REGULATION: Under non-stress conditions, Spx is degraded by
CC ClpXP (PubMed:16788195). Efficient degradation by ClpXP requires the
CC adapter protein SpxH/YjbH (PubMed:32117138). Function, levels and
CC solubility of Spx are affected by SpxH/YjbH aggregation and stress
CC conditions (PubMed:32117138). {ECO:0000269|PubMed:16788195,
CC ECO:0000269|PubMed:32117138}.
CC -!- SUBUNIT: Interacts with the C-terminal domain of the alpha subunit of
CC the RNAP. {ECO:0000255|HAMAP-Rule:MF_01132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01132}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene renders the cells
CC hypersensitive to a wide range of stress conditions including high and
CC low temperature, high osmolarity and hydrogen peroxide
CC (PubMed:16788195). Inactivation also enhances biofilm formation
CC (PubMed:16788195). {ECO:0000269|PubMed:16788195}.
CC -!- SIMILARITY: Belongs to the ArsC family. Spx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01132}.
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DR EMBL; CP000253; ABD30059.1; -; Genomic_DNA.
DR RefSeq; WP_000258003.1; NZ_LS483365.1.
DR RefSeq; YP_499487.1; NC_007795.1.
DR AlphaFoldDB; Q2G1U6; -.
DR SMR; Q2G1U6; -.
DR STRING; 1280.SAXN108_0993; -.
DR EnsemblBacteria; ABD30059; ABD30059; SAOUHSC_00934.
DR GeneID; 3920763; -.
DR GeneID; 66839191; -.
DR KEGG; sao:SAOUHSC_00934; -.
DR PATRIC; fig|93061.5.peg.855; -.
DR eggNOG; COG1393; Bacteria.
DR HOGENOM; CLU_116644_1_1_9; -.
DR OMA; IMIDDKR; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR HAMAP; MF_01132; Spx; 1.
DR InterPro; IPR006660; Arsenate_reductase-like.
DR InterPro; IPR023731; Spx.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006504; Tscrpt_reg_Spx/MgsR.
DR PANTHER; PTHR30041; PTHR30041; 1.
DR Pfam; PF03960; ArsC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01617; arsC_related; 1.
DR PROSITE; PS51353; ARSC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; Redox-active center; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..131
FT /note="Global transcriptional regulator Spx"
FT /id="PRO_0000451566"
FT DISULFID 10..13
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01132"
SQ SEQUENCE 131 AA; 15441 MW; 89F67A54666699BF CRC64;
MVTLFTSPSC TSCRKAKAWL QEHDIPYTER NIFSEHLTID EIKQILKMTE DGTDEIISTR
SKTYQKLNVD IDSLPLQDLY SIIQDNPGLL RRPIILDNKR LQVGYNEDEI RRFLPRKVRT
FQLQEAQRMV D
