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Database: UniProt
Entry: A0A1B7LHR1_9FIRM
LinkDB: A0A1B7LHR1_9FIRM
Original site: A0A1B7LHR1_9FIRM 
ID   A0A1B7LHR1_9FIRM        Unreviewed;       453 AA.
AC   A0A1B7LHR1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=A6M21_05020 {ECO:0000313|EMBL:OAT85841.1};
OS   Desulfotomaculum copahuensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT85841.1, ECO:0000313|Proteomes:UP000078532};
RN   [1] {ECO:0000313|EMBL:OAT85841.1, ECO:0000313|Proteomes:UP000078532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMa1 {ECO:0000313|EMBL:OAT85841.1,
RC   ECO:0000313|Proteomes:UP000078532};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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: 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:OAT85841.1}.
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DR   EMBL; LYVF01000047; OAT85841.1; -; Genomic_DNA.
DR   RefSeq; WP_066666581.1; NZ_LYVF01000047.1.
DR   AlphaFoldDB; A0A1B7LHR1; -.
DR   STRING; 1838280.A6M21_05020; -.
DR   OrthoDB; 9803970at2; -.
DR   Proteomes; UP000078532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   PANTHER; PTHR32071:SF113; SASR; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078532};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          5..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          142..369
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   453 AA;  50632 MW;  C8A909D48FCF2485 CRC64;
     MKHPTILIID DEEQLCWALE RALRQEGYSV LTATGGRHGL ALIQEKNPSL VVLDLKMPEM
     DGLEVLKRAR KLQPKLPVIM LTAHGTMESA IEAMKLGAAD FIAKPFDLTE LKLVIKQNLK
     VSHLVNEVDF WRAELTNKYS NMIGNSPAIR EVVQLIERVA ASNATVLITG ESGTGKEVAA
     VAIHQNSLRH KGPFVAINCA ALPEQLLESE LFGHEKGAFT GAAGRKLGRF ELADQGTIFL
     DEIAEMPMAM QVKLLRVLQE KSFERVGGTE TVHVDVRVIA ATNRNLAQAI EKGLFREDLF
     YRLNVFQIKL PPLRERKEDI PLLADHFLSR LKHAYPAQSI SPAAMEQLVK YHWPGNVREL
     QNVIERAAII CQGDEIKPEH LPKELITSPR NEDGLVVRFP DEGISLETVE KELIMQALEK
     SNGNQTRAAQ LLGITRSALL YRAQKYGLNT ERF
//
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