ID B2TJV2_CLOBB Unreviewed; 784 AA.
AC B2TJV2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=CLL_A1491 {ECO:0000313|EMBL:ACD24559.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24559.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) 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; CP001056; ACD24559.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TJV2; -.
DR KEGG; cbk:CLL_A1491; -.
DR HOGENOM; CLU_000445_70_50_9; -.
DR Proteomes; UP000001195; 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 CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 1.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF71; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 1..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 189..253
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 247..292
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 315..371
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 398..524
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 533..784
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT MOD_RES 43
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 784 AA; 90142 MW; 427FFF39E28D6448 CRC64;
MDKTQLVIVS SNAKKFLQIS NKAEESGLNF SINESIDDVI KLDINLVIID TNIGNKEVIR
SIKKLRNAFL KVRLGIIICI DKEDIENLKE YIEIGADDYI LKPFSFEEID LRISNQIKLM
KAQINSKIKD IQFDALLNNT PFMAWFKDKD SNYIKVNNEF MEHCGKTMKQ IKGKGDQYVW
SGMIGDRCRQ FDLEVMNKRT QVVFDEIIPG EKGFKQFNMY KAPVINEFDE IIGTIGIARD
ITDLKNKDAK LQMLMDNLPF PVWLTDINAK YVNGNKKFSD YFNVSMNELI GRIPHEFFGE
DIVKDIYSQN KEVMGAKETR KFESDIKVNN EIRSVEIYKT PVLDIGNEVI GIASALIDIT
DIKEAQRKIK KQAFTDALTQ ISNRTALYDY MKNESDYSNI GMMLVDIDNF KDINDYYGHN
FGDKVIVHVA NELKKICNDT FICRFGGDEF LVVFKDVESE NIICDKAEKI LEKIHMYKGH
DFSVSIGIAI GNNISDINRL LVNVDLAMYK SKELGKNRYM KYTKELEAEK NLTLNIEKDL
KYAIGKNEVK VFYQPQYTID RKLKGFEALF RWQSKKYANV PVINIIEVME SSNLIIDMGY
YIMQEACKFA KKINENRKDK IVVSINISAI QIMEKDFIKK VKSIINKTSV FIDCIGIEIT
ETVLVKNIEE NIMKIKELKD MGVTISLDDF GTGYSSLNYI VNMPLSLIKI DKSFISGMNV
KKEYTKLLRL IIASAHSLNL PIVAEGVETE EQLAKLNKMN VDYVQGFLFS KPVEEEKAFK
LLEL
//
