ID E2ZMK0_9FIRM Unreviewed; 265 AA.
AC E2ZMK0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=HMPREF9436_02920 {ECO:0000313|EMBL:EFQ05591.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05591.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ05591.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05591.1,
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:EFQ05591.1}.
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DR EMBL; AECU01000213; EFQ05591.1; -; Genomic_DNA.
DR AlphaFoldDB; E2ZMK0; -.
DR STRING; 748224.HMPREF9436_02920; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_2_9; -.
DR BioCyc; FCF748224-HMP:GTSS-938-MONOMER; -.
DR Proteomes; UP000006028; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR046947; LytR-like.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR37299:SF1; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR PANTHER; PTHR37299; TRANSCRIPTIONAL REGULATOR-RELATED; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00850; LytTR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 29..145
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 155..241
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 82
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 265 AA; 30383 MW; B51C871953E2162B CRC64;
MADHGRRNLC YNIKNREAEG TGGAAMNLRT AIVEDSKPDA ERLKQLLKKA FENENISCSC
FASGDEFLRA GGREGYQVVF LDICMEGTNG IETAQRLRAA DPDLLIVFVT SSPEYVWDAF
PVHPFDYLLK PYKEEKFEQL AGELRRVLCR QQPELEVRIA RQIVRLPLTK IYYATAQNHY
VRVVTDDGEC RATANFAQVQ EQLQTQPEFL VCNRGVIINM SKVLRFEGDC IEMLDGTHLP
VRQKDKNSLL AQFTQYQFRG MQREF
//
