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Database: UniProt
Entry: B1C9J1_9FIRM
LinkDB: B1C9J1_9FIRM
Original site: B1C9J1_9FIRM 
ID   B1C9J1_9FIRM            Unreviewed;       968 AA.
AC   B1C9J1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=ANASTE_02284 {ECO:0000313|EMBL:EDS72562.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72562.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS72562.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72562.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS72562.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72562.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) 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};
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:EDS72562.1}.
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DR   EMBL; ABIL02000006; EDS72562.1; -; Genomic_DNA.
DR   RefSeq; WP_007051032.1; NZ_DS560019.1.
DR   AlphaFoldDB; B1C9J1; -.
DR   STRING; 445971.ANASTE_02284; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_21_9; -.
DR   OrthoDB; 9804263at2; -.
DR   Proteomes; UP000005178; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 3.10.450.50; -; 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; 1.
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; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; 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; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 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:UP000005178};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          464..687
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          707..827
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          846..967
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         761
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         898
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   968 AA;  111161 MW;  EE57BC211BF7842F CRC64;
     MGRLNKKEVI AFARKILRTY FVESRLDFLI STFDDDIIWL GGGRMQKAEG KEDVANWFIS
     GKNDMFPCVM ENEDYQYMRL GDDYHMVEGV SDLYTSDNTE HIMFASQRIT FIFKEEDRKL
     KTVHIHNSIP FDELKDEELF PVEYSKEQYD LLHEAYENKL SEIDSANEAI KNQAMLLNRL
     YQSVPSGILQ LECEYPHNII IANHKIGQIY GIDEKDIKSG NYYNLLYKKI IESEDNISKV
     LHNGGVIDYE REIIKYNKEK AWISVHLDVL NDVGGNDVIQ CVINDITKQK HALIEKENEQ
     KLENSLLRSA IFSSNEAILN LNLTADTYSI ITSFEEVESD YRNIPRSGRY DDLIDKSCDL
     MVHPDYKEEY RIKFDRQNVI KQFKSGKKEI YMELMELGED GEYHWKSYTF TRAENIYNED
     IIGISIVKSL DKQRSERIRS EQLLKDALNA ARTANEAKSD FLSRMSHDIR TPLNAIIGMS
     TIGKLKIEKP NSVLDCFSKI DSSSKYLLSL INDILDMSKI ESGKVTLNDE RFDFSEMIHE
     INEIIYDQAV EKGIEYKVYS DINMDKYYIA DRLKLNQIFM NLLSNSLKYF SKGDFIHFSF
     KEVKRERGVS LIEFIVEDSG CGMSKGFLDK LFLPFEQENA GVARNNVGTG LGLTIVKNIV
     DIMEGNIEVI SEKGRGSKFI VTLPLGIIES EEEAEYRKKK ELLKGLNVLI ADDDEIVAKQ
     IEVIMNDIGA EAVKVNSGSA AVDEVKKKYE NDEFFDVCFI DWKMPDMNGI ETTGNIRRIV
     GEDTTIIIIT AYDWSVIEDE GRRAGVNHFI SKPVFEHTIC DYLTDIDVKH IRHRHKKSAK
     SLKGRNVLLV KDNILNQEIA KSILEMRGMN VDTAENGKEA VDKFIKSDIG YYDMILMDIR
     MPVMDGIEAT KAIRSSSHHR AQDIPIIAVS ANAFKEDKIK AFDAGINGYL IKPFDAGNMM
     DMIEKFLN
//
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