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
//