ID A0A371IM92_9FIRM Unreviewed; 383 AA.
AC A0A371IM92;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=BBG48_003260 {ECO:0000313|EMBL:RDY21612.1};
OS Criibacterium bergeronii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Criibacterium.
OX NCBI_TaxID=1871336 {ECO:0000313|EMBL:RDY21612.1, ECO:0000313|Proteomes:UP000093352};
RN [1] {ECO:0000313|EMBL:RDY21612.1, ECO:0000313|Proteomes:UP000093352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY21612.1,
RC ECO:0000313|Proteomes:UP000093352};
RX PubMed=27587833;
RA Maheux A.F., Berube E., Boudreau D.K., Raymond F., Corbeil J., Roy P.H.,
RA Boissinot M., Omar R.F.;
RT "Draft Genome Sequence of Criibacterium bergeronii gen. nov., sp. nov.,
RT Strain CCRI-22567T, Isolated from a Vaginal Sample from a Woman with
RT Bacterial Vaginosis.";
RL Genome Announc. 4:e00959-16(2016).
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:RDY21612.1}.
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DR EMBL; MBEW02000005; RDY21612.1; -; Genomic_DNA.
DR RefSeq; WP_068911890.1; NZ_MBEW02000005.1.
DR AlphaFoldDB; A0A371IM92; -.
DR STRING; 1871336.BBG48_05825; -.
DR Proteomes; UP000093352; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR44591:SF14; SPORULATION INITIATION PHOSPHOTRANSFERASE F; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000093352}.
FT DOMAIN 4..122
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 383 AA; 43505 MW; 098173D4B72C76C0 CRC64;
MNNTVLIVDD SFLNRVMMKE LLQKNLDDIN FLEAENGQDA FTILNEKEVD LMILDLNMPI
MDGYEVLKKI KADERMINLP IIVNSSVTDY EKMAYAISLG ARDFFTKTKA SEEMGIILST
KVKNILEYSH KINDILYLNK LQQLDMDISS KIQKSFVKDI VENGDLDISV HYQPKDMLSG
DIISSISTNS GKNYLLLVDM QASSISSVLM AVLFRELFMK KARHAESASK LMQDLNDDFI
VLTEDLNQHI LFSAFIAQFD ENGLSVCNAG FSTIPFIFYS NNAGIEKIVS SGKMIGMNKG
TKYSLVNYEL SKGDAVVFYT NGLFQEDEPM DINKLQSYFE ELYANITDKD KLDTKDITEQ
IRAHFVDENF IQDEDLTIAT IKK
//
