ID G8TSI9_SULAD Unreviewed; 353 AA.
AC G8TSI9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN OrderedLocusNames=Sulac_3235 {ECO:0000313|EMBL:AEW06681.1};
OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=679936 {ECO:0000313|EMBL:AEW06681.1, ECO:0000313|Proteomes:UP000005439};
RN [1] {ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA Gehrich-Schroeter G., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM
RT 10332.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW06681.1, ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RX PubMed=23407703; DOI=10.4056/sigs.2736042;
RA Anderson I., Chertkov O., Chen A., Saunders E., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Han C., Tapia R.,
RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA Pati A., Palaniappan K., Land M., Pan C., Rohde M., Pukall R., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Mavromatis K.;
RT "Complete genome sequence of the moderately thermophilic mineral-sulfide-
RT oxidizing firmicute Sulfobacillus acidophilus type strain (NAL(T)).";
RL Stand. Genomic Sci. 6:1-13(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:82795; EC=3.1.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00000941};
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DR EMBL; CP003179; AEW06681.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TSI9; -.
DR STRING; 679936.Sulac_3235; -.
DR KEGG; sap:Sulac_3235; -.
DR PATRIC; fig|679936.5.peg.3346; -.
DR HOGENOM; CLU_000445_51_0_9; -.
DR Proteomes; UP000005439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR008248; CheB-like.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR PANTHER; PTHR42872:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000005439}.
FT DOMAIN 14..130
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 157..349
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 64
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 353 AA; 38003 MW; D40D0DB5D2B37B3D CRC64;
MLTGMNEAED RGVRVVVVDD SAFFRYELGS RLVRRGWQLV ASVASGEEAL KVVPLLQPDL
VMMDVVMPGM GGMAAVRALR RRWPGLILMM SGQSDTGTAA TWDALEAGAN DFIPKPHADQ
TLDAMVRQIV DRYRALAPRG SEGPQPEKGT TFDKEPRTEG FKAIVIGAST GGPQALSFLL
ETIRLAPRIP VLIVQHMPSG FTRSFAERLA DRLGYPVQES PPEGDMVPWD PPPVIVAAGG
KHLRVSRQGA WSESGERLHG VIPSVDVTLS DAVSVFGRDL GVVILTGMGE DGAQGALAVH
QRGGTVIAES RETALVWGMP RAVFEAGAAD AVWPLGRISL WLRQVIQHGV PLR
//
