ID R6LS88_9CLOT Unreviewed; 304 AA.
AC R6LS88;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=BN565_01001 {ECO:0000313|EMBL:CDB88800.1};
OS Clostridium sp. CAG:253.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262785 {ECO:0000313|EMBL:CDB88800.1, ECO:0000313|Proteomes:UP000018071};
RN [1] {ECO:0000313|EMBL:CDB88800.1, ECO:0000313|Proteomes:UP000018071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:253 {ECO:0000313|Proteomes:UP000018071};
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:CDB88800.1}.
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DR EMBL; CBEI010000016; CDB88800.1; -; Genomic_DNA.
DR AlphaFoldDB; R6LS88; -.
DR STRING; 1262785.BN565_01001; -.
DR Proteomes; UP000018071; 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}.
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 304 AA; 33611 MW; 0FF7095729D9445B CRC64;
METGILLESG TNELEILEFR VADNYYGINV AKIREIISFQ TPTPIPNADS RIEGIFMPRD
EIISIIDLAE CLHLPKPETP AGDMYIVTNF NKLNTAFHVN GVLGIHRVSW SDIVKPDSTI
NTAGEGMATG IVRIDGKLII ILDFEKIVSD INPETGLKIS DVERMTHRTR NETPILIAED
SALLSKMIVN CLEQAGYTNI TTTANGQECW EKLQEYNASG DLDSKVACII TDIEMPQMDG
HHLTKLVKDD PDMNHLPVII FSSLVNEEMK IKGKQLGADA QLSKPEIGQL VSEIDKLVGN
VQAE
//
