ID   SPX_LACLM               Reviewed;         132 AA.
AC   P60376; A2RIZ4; Q9ETA4;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Global transcriptional regulator Spx {ECO:0000255|HAMAP-Rule:MF_01132};
GN   Name=spx {ECO:0000255|HAMAP-Rule:MF_01132}; Synonyms=nrpR, spxA;
GN   OrderedLocusNames=llmg_0640;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10048028; DOI=10.1046/j.1365-2958.1999.01222.x;
RA   Duwat P., Ehrlich S.D., Gruss A.;
RT   "Effects of metabolic flux on stress response pathways in Lactococcus
RT   lactis.";
RL   Mol. Microbiol. 31:845-858(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9987112; DOI=10.1046/j.1365-2958.1999.01149.x;
RA   Frees D., Ingmer H.;
RT   "ClpP participates in the degradation of misfolded protein in Lactococcus
RT   lactis.";
RL   Mol. Microbiol. 31:79-87(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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, ECO:0000305}.
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DR   EMBL; AF058950; AAG43111.1; -; Genomic_DNA.
DR   EMBL; AF028804; AAG37358.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97242.1; -; Genomic_DNA.
DR   RefSeq; WP_003129597.1; NC_009004.1.
DR   AlphaFoldDB; P60376; -.
DR   SMR; P60376; -.
DR   STRING; 416870.llmg_0640; -.
DR   PaxDb; 416870-llmg_0640; -.
DR   GeneID; 61108935; -.
DR   GeneID; 89632775; -.
DR   KEGG; llm:llmg_0640; -.
DR   eggNOG; COG1393; Bacteria.
DR   HOGENOM; CLU_116644_1_1_9; -.
DR   OrthoDB; 9794155at2; -.
DR   PhylomeDB; P60376; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd03032; ArsC_Spx; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   NCBIfam; TIGR01617; arsC_related; 1.
DR   NCBIfam; NF002459; PRK01655.1; 1.
DR   NCBIfam; NF009885; PRK13344.1; 1.
DR   PANTHER; PTHR30041; ARSENATE REDUCTASE; 1.
DR   PANTHER; PTHR30041:SF7; GLOBAL TRANSCRIPTIONAL REGULATOR SPX; 1.
DR   Pfam; PF03960; ArsC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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..132
FT                   /note="Global transcriptional regulator Spx"
FT                   /id="PRO_0000162555"
FT   DISULFID        10..13
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01132"
SQ   SEQUENCE   132 AA;  15030 MW;  F63EE4B8204136B3 CRC64;
     MITIYTAPSC TSCKKAKTWL SYHHIPFNER NLIADPLSTT EISQILQKCD DGVEGLISSR
     NRFVKTLGVD FEDISLSQAI KIISENPQIM RRPIIMDEKR LHVGYNEEEI RAFLPRTVRV
     LENGGARLRS AI
//