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Database: UniProt
Entry: F6B735_DESCC
LinkDB: F6B735_DESCC
Original site: F6B735_DESCC 
ID   F6B735_DESCC            Unreviewed;       808 AA.
AC   F6B735;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   OrderedLocusNames=Desca_1607 {ECO:0000313|EMBL:AEF94460.1};
OS   Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS   (Desulfotomaculum carboxydivorans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94460.1, ECO:0000313|Proteomes:UP000009226};
RN   [1] {ECO:0000313|EMBL:AEF94460.1, ECO:0000313|Proteomes:UP000009226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC   {ECO:0000313|Proteomes:UP000009226};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA   Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT   "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF94460.1, ECO:0000313|Proteomes:UP000009226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC   {ECO:0000313|Proteomes:UP000009226};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA   Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT   "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL   Submitted (MAY-2011) 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; CP002736; AEF94460.1; -; Genomic_DNA.
DR   RefSeq; WP_013810277.1; NC_015565.1.
DR   AlphaFoldDB; F6B735; -.
DR   STRING; 868595.Desca_1607; -.
DR   KEGG; dca:Desca_1607; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_000445_11_4_9; -.
DR   Proteomes; UP000009226; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd17534; REC_DC-like; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR46663; DIGUANYLATE CYCLASE DGCT-RELATED; 1.
DR   PANTHER; PTHR46663:SF2; GGDEF DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 4.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009226}.
FT   DOMAIN          11..126
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          207..259
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          260..315
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          339..389
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          390..426
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          463..514
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          677..806
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   COILED          373..400
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         61
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   808 AA;  92080 MW;  6DAE0EC2CF463920 CRC64;
     MQVENMQKRK KILLVEDSRL TAMVVAGLLN KNGYETETAV TGEEAVQKIS GGSLPDLVLM
     DIELAGKMDG IDAARRILKS RDIPVIFLTA NASREILENI KAVKGYGFVV KGSDKYALLS
     TVEMALKLHE ANTHARMFER LFENSLNELY IFHPKSLKYV AVNRAARKNL GYTIEELNTM
     IPLDLKPEFD IESFQKILNP LVSGEQEQVL FNTVHRRKDG SLYPVEINLQ LFDYGGEKLC
     LALVVDLTER RAMEEELKEK ETTLSAIMGS AREAIVMLDG QGNVIFWNPA AELLFGYSRE
     EILGKDLHRL VVPDECLYQA YNKAFKHFQL TGEGKAVGKT MELKTKHKDG RELDVELSLS
     ALRFRNAWHA VGIVRDISER KQAQEELENS RKQYLELAEN APIGILKCDQ EGNIIYVNQK
     TLEMLGSPSI EETKKINLLT FPLLVRYGLS RKLEECLQNN KPGTYEMNYE SKWGKKVWLR
     VHIKPQVDRN TVIGAQIIID DITERKQLEE VNRRKEERFR LMLEGIPNPA WLVSRKRRIL
     AQNKAASALF GTKVGDYCWK RVLGGGNLPD EYREAYEKNG SPLPGTKCYF CRGDEALAGN
     KPLNSEVELG GNIWDMWWIP LGEDVYLHYA TDVTRYKKIE EELRQLSVTD VLTNAYNRRY
     FTQKLEEEIE RAKRADRKFS LIILDIDRFK SINDRFGHNA GDLVLKSIAE LIKNRIRKID
     TLARWGGEEF VILLPDTTVK NAARLAEELR ESLSQMDIPG VDHVTASFGV AGYCPGDMVD
     TLVNKADNMM YEAKAAGRNC VRYMNECE
//
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