ID F0T1K5_SYNGF Unreviewed; 477 AA.
AC F0T1K5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=Sgly_3163 {ECO:0000313|EMBL:ADY57429.1};
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57429.1, ECO:0000313|Proteomes:UP000007488};
RN [1] {ECO:0000313|EMBL:ADY57429.1, ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX PubMed=21886864;
RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT (FlGlyR).";
RL Stand. Genomic Sci. 4:371-380(2011).
RN [2] {ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-2011) 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; CP002547; ADY57429.1; -; Genomic_DNA.
DR AlphaFoldDB; F0T1K5; -.
DR STRING; 645991.Sgly_3163; -.
DR KEGG; sgy:Sgly_3163; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG2206; Bacteria.
DR HOGENOM; CLU_000445_92_10_9; -.
DR OrthoDB; 9798833at2; -.
DR Proteomes; UP000007488; Chromosome.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00077; HDc; 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; IPR021800; DUF3369.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00277; HDIG; 1.
DR PANTHER; PTHR45228:SF1; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186; 1.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR Pfam; PF11849; DUF3369; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000007488}.
FT DOMAIN 13..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 302..477
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 324..446
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 477 AA; 54067 MW; 67956DFCD808E923 CRC64;
MRRSKANPIL DYKILVVDDE QGIVDSLSVV LKRSGYQITG LTDPLEAIEK VRQENFDLLI
LDFLMFPIHG DKVVEKIRQF NTDIYILMLT GHKDLAPPLE TIKALDIQGY CEKGDRLDQL
LLLVESGIKS ISQMRTIRIF QEGLNKILQA VPKIYQLQPI DNILEDILSE ILPLINSKNA
FILVDDVTRI SSGNNSIYKG IGKYKTEIED FMVMLDPSLM EHIGSARVDK KVVILEREVI
IPLINELQQD IGVIYVEGEG IQEGSKLLEI YASQAASSIS NAFLHSLVNI KNDELNMTYD
QLKERYMDTI EALRLVVDAK DIYTRGHSER VAYFAVKIGQ SFGLSQEELE LLRISGIFHD
VGKIGTSDDI LFKSEKLDEK EYEEIKKHPL KGAHILSAIS MFKEVVPIVK CHHERVDGKG
YPEGLKKEEI PFLARIISVA DAFDAMMSDR HYRSKLKFEE ARAQLLQGAG TQCTQTR
//
