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Database: UniProt
Entry: A0A1M4WYD2_9CLOT
LinkDB: A0A1M4WYD2_9CLOT
Original site: A0A1M4WYD2_9CLOT 
ID   A0A1M4WYD2_9CLOT        Unreviewed;       920 AA.
AC   A0A1M4WYD2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN02745158_01798 {ECO:0000313|EMBL:SHE86218.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE86218.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHE86218.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE86218.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; FQVI01000007; SHE86218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4WYD2; -.
DR   STRING; 1122155.SAMN02745158_01798; -.
DR   Proteomes; UP000184245; Unassembled WGS sequence.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd01948; EAL; 1.
DR   CDD; cd01949; GGDEF; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.20.20.450; EAL domain; 1.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00254; GGDEF; 2.
DR   PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR   PANTHER; PTHR33121:SF70; CYCLIC DI-GMP PHOSPHODIESTERASE PDEH; 1.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF00990; GGDEF; 2.
DR   Pfam; PF00072; Response_reg; 2.
DR   SMART; SM00052; EAL; 1.
DR   SMART; SM00267; GGDEF; 2.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS50883; EAL; 1.
DR   PROSITE; PS50887; GGDEF; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000184245}.
FT   DOMAIN          43..160
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          200..328
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   DOMAIN          336..590
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
FT   DOMAIN          617..733
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          775..906
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   MOD_RES         93
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   920 AA;  104471 MW;  AD74DC653A81BFFC CRC64;
     MVKKHKDRPD SGSANCKDSK VYTDTFEVTE ENGGDIQMPM LKTVLIVEDN EINRGVLHNL
     LASAYQVLEA DNGQAALEVL QSRHEEISLI LLDINMPVMD GYTFLSHIKA NSSFSSIPVI
     VTTQSDSEAD EVSALSHGAS DFVPKPYKAR IILHRVASII RLRETAAMIN QFQYDRLTGL
     YSKEYFYQRV REIFQQYPER QFDLIASDIE NFKLINDILG VAAGDRLLQG IAGQYRQMVG
     DKGICGRLNA DQFVCLLENN KVYTADMFAS TLEQVNALPN AQNVVMKWGI YYVEDRTLPV
     EQMCDRALLA ARSIKGQYGK HFAAYDDKLR GELLRQQAII DGMETALSEG QFMLYLQPKY
     RIRDNKLVGA EALIRWNHPI WGFQLPAEFI PLFEKNGFIA KLDQFVWDKA CSTLREWDEK
     GYLPISISVN VSRADIYNIN IIEILMDTVR RHGLRPSRLH LEITESAYTE QPAQIIETIT
     KLRELGFIIE MDDFGSGYSS LNMLNQMPLD ILKLDMKFIQ GETGKSVGQG ILQTIVELAR
     RMRLSVVAEG VETKEQLDRV AETGCDYVQG YYFAKPMPIQ DLEALLKERR AAELLVEDND
     CIAAPHFGMR LRPLRQLLLI ADVDQEYRKE VEKTFSRHFQ VIHSTEADST LTFVTQYKDQ
     LAAVLISKSL PGLDGFTVFE MLKDELEVWN IPVLVTGAQD SEAEERALEL GAFDYADKPH
     TAKSLLKRTL KAIRLSSFQE REHALQNEAN RDHMTGFLNR RGLEAAIHTM GKEDTPFAFC
     LFDLDDLKKT NDTLGYTEGD RIIQEITRLI RAQSRKSDIL ARYGGDEFIV ILKQIQSADV
     VVKRVEGICR ALKKNTFEQD IQASASAGIV ISENLENGMD EVFRQADMAL YRAKTNHKGS
     SCLWRNEDES LQGFKENARE
//
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