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Database: UniProt
Entry: E2ZM19_9FIRM
LinkDB: E2ZM19_9FIRM
Original site: E2ZM19_9FIRM 
ID   E2ZM19_9FIRM            Unreviewed;       233 AA.
AC   E2ZM19;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=HMPREF9436_02730 {ECO:0000313|EMBL:EFQ05785.1};
OS   Faecalibacterium cf. prausnitzii KLE1255.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05785.1, ECO:0000313|Proteomes:UP000006028};
RN   [1] {ECO:0000313|EMBL:EFQ05785.1, ECO:0000313|Proteomes:UP000006028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05785.1,
RC   ECO:0000313|Proteomes:UP000006028};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) 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:EFQ05785.1}.
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DR   EMBL; AECU01000201; EFQ05785.1; -; Genomic_DNA.
DR   RefSeq; WP_005945175.1; NZ_GL538344.1.
DR   AlphaFoldDB; E2ZM19; -.
DR   STRING; 748224.HMPREF9436_02730; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_4_9; -.
DR   OrthoDB; 9790442at2; -.
DR   BioCyc; FCF748224-HMP:GTSS-1914-MONOMER; -.
DR   Proteomes; UP000006028; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17574; REC_OmpR; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.690; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF40; SENSORY TRANSDUCTION PROTEIN REGX3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          132..231
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        132..231
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   233 AA;  26526 MW;  8A4C51A260A8C3B9 CRC64;
     MNSVLIIDDD KKLCALMKKC VEQENLSAVV AHGGLEGLRL LEKNKDTCSL IILDVMMPDM
     NGFQVLQKIR EKNNVPVLML TAKSDEEDKV SGLRLGADDY LTKPFGINEL MARVNSLIRR
     YTTLNPVTGN EAATMLLKDM VIDKINRTVT VQNLPVDLTG KEFDLLLFLA SNKGRVFTKK
     QLYTQVWTEE YDFDDNNLMA FISKLRKKIE PNPEQPFYIQ TVRGVGYRFN KEA
//
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