ID A0A1I5VH82_9FIRM Unreviewed; 306 AA.
AC A0A1I5VH82;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02910358_00577 {ECO:0000313|EMBL:SFQ06346.1};
OS Lachnospiraceae bacterium XBB1006.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFQ06346.1, ECO:0000313|Proteomes:UP000199554};
RN [1] {ECO:0000313|EMBL:SFQ06346.1, ECO:0000313|Proteomes:UP000199554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB1006 {ECO:0000313|EMBL:SFQ06346.1,
RC ECO:0000313|Proteomes:UP000199554};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOXT01000005; SFQ06346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5VH82; -.
DR STRING; 1520827.SAMN02910358_00577; -.
DR OrthoDB; 9806105at2; -.
DR Proteomes; UP000199554; 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:UP000199554}.
FT DOMAIN 13..151
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 172..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 306 AA; 34158 MW; 6F01B5A4FC32D684 CRC64;
MDTNILLENG TNEVEILEFV LGDNHYGINV AKIREILTYQ PVTPIPNGHY CVEGIFMPRD
TMITVISLRE CLGLKPGEDK GLFIITNFNK LDIAFHVDRV IGIHRISWAD IIKPDSTINA
ENNGVSTGVV KFDDKLVVIL DFEKIVTDIS PDTGLKVTDI ENYEGRDRSM CPIVIAEDSP
MLGRMITDCL KKSGYTKLTL CENGQIAWDT LCELRDAGAG NLYSKVKCII TDIEMPIMDG
HRLTKLCKED EVIKEIPLVI FSSLVNEEMR RKGEQLGADA QLTKPEIGML VDAIDRLIDE
SSLSNN
//
