ID A0A1H3WW70_9FIRM Unreviewed; 1209 AA.
AC A0A1H3WW70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04515656_101115 {ECO:0000313|EMBL:SDZ91379.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SDZ91379.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SDZ91379.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SDZ91379.1,
RC ECO:0000313|Proteomes:UP000199394};
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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; FNRK01000001; SDZ91379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3WW70; -.
DR STRING; 81409.SAMN04515656_101115; -.
DR OrthoDB; 9804263at2; -.
DR Proteomes; UP000199394; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 24..99
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 102..153
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 231..284
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 699..922
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 942..1062
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1083..1204
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 996
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1135
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1209 AA; 137518 MW; 263A89E01A69F117 CRC64;
MNKKKTGGKR FSHESAATKN FDANQIQLQN IINAIPGGVA IYRVTDIFET VYFSDGVPAL
TGYTVEEYRE RIKGDAAVMT HPEDTARVVK ELNRALEDGT VADFDFRKTH RDGSIVWVHL
QGCRIGEEDG APLLQCVFHN ITRQKAIEQK LREKEAIYDI AMDNTDVNIW RYDIYSDCLT
QFPQSVKAHA GFPQKIENFI QTVLDSGFVK PESRQDFRQL YERVSQGEDN VSEDIWFATE
DGKGWWCERI RHSIIRDDTG RPLYAIGVGR NITQEMKALV EKQQMELAIS STSISMWTYD
IQTGVYQSNN QGESNNQGAE NIGFFASSPG GYTRIIELGY VAPESELDFI KLHHSLEQGQ
PSATAIIRYN TLKTPVEWQR ITYSTIFSNA GEPVIGVAVG EDITEFMNAK KRFSDELHFQ
EQDITGNVLV KVRSNLTQDR VERYMARDTV GISHDGMTYT VGVQALAATG YTQKEQDHIR
YMLNAQRVMK AFEKGDTSYS LDYQRKSHDG RVIWVNTMVR TFQDPESGDI KSFMYTYDID
QERTTQLLIN RLIDIDFEFL GIIDTAQETL YCMRHNMVGH RYGTGILVDY EEATGNTIDK
YIVSDQREMI REAFALSTIK QRLEKDDAYS CTFSVEIEGE EYRKRWKYTY LDESRTRIVM
IRSDVTELFF QQERQQGILR EALKQAEQAS VAKTEFLSRM SHEIRTPMNA IIGMSALAAQ
NVEDRKQVTD YLSKVGISAR FLLSLINDIL DMSRIESGKI TIKEEEIPFE EFIADINAIG
YELASGKEVD YDCMITSFVE QSYLGDAMKL QQIIINLISN AVKFTPAGGK VQFIVHQSGV
NDGKAHLRFT VNDTGIGISE SFMPRIFDPF EQQHSGSTSP YGGTGLGLAI CKNLVELMGG
TIAVNSIEGV GTEFTVDITL GINADKKHLY QLKSQINWNS LSILIVDDEV GICRQTQRIF
QEMGAVAEWV ESGQKALDKV EKRQLRQQSY DVILIDWKMP EMDGIETTRR IRQLVGPDVT
IIIMTAYDWA SIETEAKMAG VNFLMTKPLF KASLCSTFEK IYNQKEREIE AIKPRSYDFK
GKRVLLVEDH ILNVEVARRL LEVKGITVEV AENGLRAIEM FTLAPVGYYD MILMDIRMPV
MDGLTATKTI RQLQKETAKT IPIVAMSANA FEEDMEKSRY AGMNYHLAKP IAPQMLYDTL
ERIWSEAKK
//
