ID R5SF21_9CLOT Unreviewed; 299 AA.
AC R5SF21;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, 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=BN771_00483 {ECO:0000313|EMBL:CCZ51743.1};
OS Clostridium sp. CAG:75.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262836 {ECO:0000313|EMBL:CCZ51743.1, ECO:0000313|Proteomes:UP000018032};
RN [1] {ECO:0000313|EMBL:CCZ51743.1, ECO:0000313|Proteomes:UP000018032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:75 {ECO:0000313|Proteomes:UP000018032};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ51743.1}.
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DR EMBL; CBAE010000023; CCZ51743.1; -; Genomic_DNA.
DR AlphaFoldDB; R5SF21; -.
DR Proteomes; UP000018032; Unassembled WGS sequence.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR024181; Chemotax_regulator_CheV.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR47233; CHEMOTAXIS PROTEIN CHEV; 1.
DR PANTHER; PTHR47233:SF3; CHEMOTAXIS PROTEIN CHEV; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002867; CheV; 1.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000018032}.
FT DOMAIN 13..153
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 174..299
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 232
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 299 AA; 33554 MW; 6F697DD461B1ABDD CRC64;
MDTNILLESG TNELEILEFV VDGHNYGINV AKIREIISYT ELTPIPNAHP FVEGAFSTRG
ETITVVNLAK CLGMNECEEK KTDMFLVTSF NGTNAAFHVH SVVGIHRVNW SQIVKPDRLI
SNSRTSMITG IINIDKHLVI LLDFENIVAQ ISPEAGIQLS DIERLGSRPK NNKPILYAED
SQFLSLMIYD GLTAAGFTNL MPLNNGLELW ELLEQYRQEG TLKEKVACVV TDIEMPQMDG
HRLLKLIKET PAYKDIPVII FSSLINEDMR RKGEQLGADA QLSKHEMAEF VKELDRVLA
//