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Database: UniProt
Entry: A0A162MRT0_9FIRM
LinkDB: A0A162MRT0_9FIRM
Original site: A0A162MRT0_9FIRM 
ID   A0A162MRT0_9FIRM        Unreviewed;       694 AA.
AC   A0A162MRT0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   Name=ydaM {ECO:0000313|EMBL:KYO67033.1};
GN   ORFNames=ATZ99_08500 {ECO:0000313|EMBL:KYO67033.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO67033.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO67033.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO67033.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO67033.1}.
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DR   EMBL; LOHZ01000023; KYO67033.1; -; Genomic_DNA.
DR   RefSeq; WP_068748001.1; NZ_LOHZ01000023.1.
DR   AlphaFoldDB; A0A162MRT0; -.
DR   STRING; 520767.ATZ99_08500; -.
DR   PATRIC; fig|520767.4.peg.943; -.
DR   OrthoDB; 9783388at2; -.
DR   Proteomes; UP000075737; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; 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; cd01949; GGDEF; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; 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; PF13426; PAS_9; 3.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
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); 3.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:KYO67033.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075737};
KW   Transferase {ECO:0000313|EMBL:KYO67033.1}.
FT   DOMAIN          15..130
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          138..181
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          263..317
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          344..394
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          395..436
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          558..687
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   MOD_RES         65
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   694 AA;  79980 MW;  D7308E92FE858812 CRC64;
     MGISENRTLD SERIKILVVD DSRLLRVMMS DLLTANGYEV RTASNSFEAI DMAFYTFSPD
     LILMDIELGD EMDGIEVAKK ILQKKDIPII FLTAKTSPEV INRIKETTAY GYLEKKVSNE
     AIISAIEMAL KLYSVNNLAS MFKHIFENSP NELLITDLQN NKFITANKNA RENLGYSEEE
     IKNLSPRDIA PEILESPIRE LIQKLCDKKE TSVAFKTYHL RKDKTTYPVQ VELNVLDYLG
     KKLCVANVQD LTYQKVFEKK LAEKDYIIKL LTDSAFDAIT VINDEGKVVF WNPAAERIFG
     YSEKEIINED VHKLIVPCYE KIENSFVDYM NYFRQKGDLS FLRNPLELMA KNKYGETIYI
     ELTLSPIKLN EKWHAVGIVR DITEKKKSQI EIENMWRMYF ELAEHAPVGI LRCDKDGNII
     YVNKKVLEIL GSPSEEETRK INLLTFPHLV GYGFSTKLKE CLENNKTIIF EVFYKSIWGK
     DFWARVHIKP HIESNKVTGA LIILDDITDR KILEEKIRRQ AIRLRRLSYT DDLTGAFNRR
     FLLKKLEEEI ERVKRYGGNF SIILLDIDNF KKINDRCGHN TGDLALKYVV KTIKERIRKA
     DTLARWGGEE FIIFLPSTPV EKATILAETL RENISRITLP CPEKVTASFG VAGFLEGDTI
     DSLIKRADDL MYRAKEKGKN CVACQKDVDH INNM
//
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