ID A0A1M5Z207_9FIRM Unreviewed; 286 AA.
AC A0A1M5Z207;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02745823_03125 {ECO:0000313|EMBL:SHI18276.1};
OS Sporobacter termitidis DSM 10068.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Sporobacter.
OX NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHI18276.1, ECO:0000313|Proteomes:UP000183995};
RN [1] {ECO:0000313|EMBL:SHI18276.1, ECO:0000313|Proteomes:UP000183995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10068 {ECO:0000313|EMBL:SHI18276.1,
RC ECO:0000313|Proteomes:UP000183995};
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; FQXV01000012; SHI18276.1; -; Genomic_DNA.
DR RefSeq; WP_073080906.1; NZ_FQXV01000012.1.
DR AlphaFoldDB; A0A1M5Z207; -.
DR STRING; 1123282.SAMN02745823_03125; -.
DR OrthoDB; 9779069at2; -.
DR Proteomes; UP000183995; Unassembled WGS sequence.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17906; CheX; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.1550.10; CheC-like; 1.
DR InterPro; IPR028976; CheC-like_sf.
DR InterPro; IPR028051; CheX-like_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
DR Pfam; PF13690; CheX; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF103039; CheC-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000183995}.
FT DOMAIN 5..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 286 AA; 31144 MW; 93D289DD6BA8EAB5 CRC64;
MKEINIVVVD DSPFSVAMIS NILTGSGFNV IGSANGLEEA VEAVKTLQPD VVTMDITMPG
ADGIECTNAI HKVVPRQKVV IVSSMMDEEI IRRAKKAKVS GYVQKPVDAE ELTLAINRVM
ADEELFIELE GLYTTVFKEA LTDSFNKLFK TVPEFEAEFK NNNAQVSRGI SVVIGIIGKY
SGRLILDMSN ETARHMAGTM MNSDALPDEY IVNIVGEVSN IAAGNACSLM NKTNKLFGLR
VAPPTIVYGE SITISKSDFD TAFSVTAQTT FGEIFMNVGF NRGEYQ
//
