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Database: UniProt
Entry: A5N561_CLOK5
LinkDB: A5N561_CLOK5
Original site: A5N561_CLOK5 
ID   A5N561_CLOK5            Unreviewed;       248 AA.
AC   A5N561;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   OrderedLocusNames=CKL_0388 {ECO:0000313|EMBL:EDK32442.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32442.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK32442.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC   -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC       be an element of the effector pathway responsible for the activation of
CC       sporulation genes in response to nutritional stress. Spo0A may act in
CC       concert with spo0H (a sigma factor) to control the expression of some
CC       genes that are critical to the sporulation process.
CC       {ECO:0000256|ARBA:ARBA00024867}.
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DR   EMBL; CP000673; EDK32442.1; -; Genomic_DNA.
DR   RefSeq; WP_011988957.1; NC_009706.1.
DR   AlphaFoldDB; A5N561; -.
DR   STRING; 431943.CKL_0388; -.
DR   KEGG; ckl:CKL_0388; -.
DR   eggNOG; COG3279; Bacteria.
DR   HOGENOM; CLU_000445_14_1_9; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR046947; LytR-like.
DR   InterPro; IPR007492; LytTR_DNA-bd_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR37299:SF1; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR   PANTHER; PTHR37299; TRANSCRIPTIONAL REGULATOR-RELATED; 1.
DR   Pfam; PF04397; LytTR; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00850; LytTR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50930; HTH_LYTTR; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT   DOMAIN          3..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          151..211
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   248 AA;  29468 MW;  8A9F3E16BD1F1FAD CRC64;
     MVNILVLEDN QVQRKILVET IRQIDKHFII YEGDSEKEGL EIANEKEISL FYVDISLKGS
     SGLDFAKKVR TIDKYKLTWI VFITTYVKYM LEAFKEVHCY DYIIKPYKKE KVREVTLTLL
     ENKKREDIKL IDEKKYVVFN VGGILLKLCV DDIIFIEVYL RTFIIHTKTG KYEAKNTSLK
     KIKEQMKYFN FIQVHKSYIV NLKLVKSIDR TTCPWNIQFE NYKECVPIGN KFKDDVLKKF
     KDNFRGVL
//
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