ID   SPX_STRMU               Reviewed;         137 AA.
AC   Q8DU17;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Global transcriptional regulator Spx {ECO:0000255|HAMAP-Rule:MF_01132};
GN   Name=spx {ECO:0000255|HAMAP-Rule:MF_01132}; OrderedLocusNames=SMU_1142c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2] {ECO:0007744|PDB:3L78}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-120.
RC   STRAIN=ATCC 700610 / UA159;
RA   Liu X., Fu T.M., Su X.-D.;
RT   "The crystal structure of SMU.1142c from Streptococcus mutans UA159.";
RL   Submitted (DEC-2009) to the PDB data bank.
CC   -!- FUNCTION: Global transcriptional regulator that plays a key role in
CC       stress response and exerts either positive or negative regulation of
CC       genes. Acts by interacting with the C-terminal domain of the alpha
CC       subunit of the RNA polymerase (RNAP). This interaction can enhance
CC       binding of RNAP to the promoter region of target genes and stimulate
CC       their transcription, or block interaction of RNAP with activator.
CC       {ECO:0000255|HAMAP-Rule:MF_01132}.
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   -!- SIMILARITY: Belongs to the ArsC family. Spx subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01132}.
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DR   EMBL; AE014133; AAN58834.1; -; Genomic_DNA.
DR   RefSeq; NP_721528.1; NC_004350.2.
DR   RefSeq; WP_002263835.1; NC_004350.2.
DR   PDB; 3L78; X-ray; 1.90 A; A=1-120.
DR   PDBsum; 3L78; -.
DR   AlphaFoldDB; Q8DU17; -.
DR   SMR; Q8DU17; -.
DR   STRING; 210007.SMU_1142c; -.
DR   PRIDE; Q8DU17; -.
DR   EnsemblBacteria; AAN58834; AAN58834; SMU_1142c.
DR   GeneID; 66817461; -.
DR   KEGG; smu:SMU_1142c; -.
DR   PATRIC; fig|210007.7.peg.1024; -.
DR   eggNOG; COG1393; Bacteria.
DR   HOGENOM; CLU_116644_1_1_9; -.
DR   OMA; IMIDDKR; -.
DR   PhylomeDB; Q8DU17; -.
DR   EvolutionaryTrace; Q8DU17; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Disulfide bond; Redox-active center;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..137
FT                   /note="Global transcriptional regulator Spx"
FT                   /id="PRO_0000162574"
FT   DISULFID        10..13
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01132"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           39..48
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           62..66
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           76..85
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:3L78"
FT   HELIX           109..113
FT                   /evidence="ECO:0007829|PDB:3L78"
SQ   SEQUENCE   137 AA;  15968 MW;  736821A9B10FCA1F CRC64;
     MVTLFLSPSC TSCRKARAWL NRHDVVFQEH NIMTSPLSRD ELLKILSYTE NGTEDIISTR
     SKVFQKLDID VDELSVSELI NLISKNPSLL RRPIIMDNKR MQIGFNEDEI RAFLPRDYRK
     QELRQATIRA EVEGEDD