ID A0A1M5BZD0_9CLOT Unreviewed; 690 AA.
AC A0A1M5BZD0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02745158_03884 {ECO:0000313|EMBL:SHF47552.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF47552.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHF47552.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF47552.1,
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}.
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DR EMBL; FQVI01000031; SHF47552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5BZD0; -.
DR STRING; 1122155.SAMN02745158_03884; -.
DR OrthoDB; 9804747at2; -.
DR Proteomes; UP000184245; Unassembled WGS sequence.
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; cd01949; GGDEF; 1.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_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; 1.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR PANTHER; PTHR45228:SF5; CYCLIC DI-GMP PHOSPHODIESTERASE VC_1348-RELATED; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51832; HD_GYP; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184245}.
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 143..351
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 544..670
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 690 AA; 79195 MW; A51F3008DBEDC3AB CRC64;
MKLQKKILIV DDSELNRSLL ADMLCDEYEI MEAENGLEAL KLMERHHFEL SLVLLDIVMP
EMDGFEVLVM MNKNEWIERI PVIIISSETA AAYTDAAYDL GATEYVNRPF DPKTIRRRVS
NTIMLYSKQK FLENAVTEQV LEKEKSNLIM VEVLSHIVEF RNGESGMHVL TIRTITEMLL
KQLCIRYAEY SYLQSEILLI ANASALHDIG KISIDEKILN KPARLTPEEY EIMKKHSLIG
ADMLEKTRHY PGEELVRIAR DICRWHHERY DGKGYPDGLV GDEIPIEAQV VSLADVYDAM
THARVYKEAY PHKEALEMIF SGYCGAFNPL LLECLRDIGP ALEKELKVRS LRYATKEEVK
EITRNLLQRG EASNRTLALL EQERIKHRFF SAMSNEILFE YDRQPDMLML SEWGAAQLKL
PEIMVHLAEN KQFRQVIKIE DYMDLRSKLR HKSPGAPTVT EKYCLCINGQ WRWFKIVARP
LWRGGDSTVV TGAIGKCTDI HDEVTQLAHL KQIASIDDVT GLYRRNYARS KVQEILGNTY
GSDKKYALMV FDLDFFKNAN DLYGHMFGDK VLEEVARRLK HSVRNSDIVA RIGGDEFLVF
VEYTNEISPV ADRVFRSLGG VYGGFVISAS MGVALFPVHA IEYSDLFQSA DQALYAAKHK
GRNCYCMYDD SMDNFLSVLS EEISYEVDAR
//
