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Database: UniProt
Entry: J7INC4_DESMD
LinkDB: J7INC4_DESMD
Original site: J7INC4_DESMD 
ID   J7INC4_DESMD            Unreviewed;       253 AA.
AC   J7INC4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   OrderedLocusNames=Desmer_1087 {ECO:0000313|EMBL:AFQ43110.1};
OS   Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS   NCIMB 13706 / S10).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ43110.1, ECO:0000313|Proteomes:UP000005262};
RN   [1] {ECO:0000313|EMBL:AFQ43110.1, ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
RN   [2] {ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA   Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT   "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003629; AFQ43110.1; -; Genomic_DNA.
DR   RefSeq; WP_014902029.1; NC_018515.1.
DR   AlphaFoldDB; J7INC4; -.
DR   STRING; 768704.Desmer_1087; -.
DR   KEGG; dmi:Desmer_1087; -.
DR   eggNOG; COG3279; Bacteria.
DR   HOGENOM; CLU_000445_14_1_9; -.
DR   OrthoDB; 9809318at2; -.
DR   Proteomes; UP000005262; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   DOMAIN          3..117
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          147..253
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   COILED          106..133
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   253 AA;  29352 MW;  E8D99EB6EB12B5BF CRC64;
     MIKIVLVDDE QPAREELRFL LEKNSEMEII GEFSSGVQTI EGIPNLQPEV IFMDVHLQDM
     DGIDVVRALQ QLDMRASVVF ATAYDVHAIR AFELNAVDYI LKPFSQERLK VTIDRIQQRI
     QSHDQELTQK ISRLIQEIGV KQRPRKLAAT SKGRVVLIDP QELLYVVAEG RYASLVTEHK
     MWPTTFSLHE IEERLDPAQF LQTHRAYIVN LDRIKEVIPW FNSTYKIIID GEKATEIPVS
     RTYIKKLKER LDV
//
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