ID R9KFE8_9FIRM Unreviewed; 859 AA.
AC R9KFE8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C809_03161 {ECO:0000313|EMBL:EOS45028.1}, FMM75_14615
GN {ECO:0000313|EMBL:NDO50570.1};
OS Lachnospiraceae bacterium MD335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS45028.1, ECO:0000313|Proteomes:UP000014081};
RN [1] {ECO:0000313|EMBL:EOS45028.1, ECO:0000313|Proteomes:UP000014081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COE1 {ECO:0000313|EMBL:EOS45028.1,
RC ECO:0000313|Proteomes:UP000014081};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDO50570.1, ECO:0000313|Proteomes:UP000543970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD335 {ECO:0000313|EMBL:NDO50570.1,
RC ECO:0000313|Proteomes:UP000543970};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) 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:EOS45028.1}.
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DR EMBL; ASSW01000050; EOS45028.1; -; Genomic_DNA.
DR EMBL; VIRA01000071; NDO50570.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KFE8; -.
DR STRING; 1235793.C809_03161; -.
DR PATRIC; fig|1235793.3.peg.3279; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_21_9; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000014081; Unassembled WGS sequence.
DR Proteomes; UP000543970; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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 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; 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; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000014081};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 594..713
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 734..855
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 648
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 786
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 859 AA; 95871 MW; 9D0D01F250C21138 CRC64;
MKRKQKKSGA DQGVSLLLSI ILVFCILGAV VFSVARKIST EMSASAIQNL SESLDLIECT
IEAILNKEAE FQTMMAQKVA VADDPKEYIE SYSKNQTMVK ISLIRAGETQ GISNTGETFS
EEGLDFSAGG AIGGLEVSRS YMNYMGTWAY TMKCPVEKDG RQIAALYVEY VYDSFDKSLP
NGFYDGKAML YIMDAQSQRM VLKPKGMGER SAGHLNLEDF FRANDILEAD LQAEVSDCIK
NAENMMFYHD IRGKSSLIYM WSVNNGTIYL IGYVPIEAIQ QEGRTVNQNI FIVVIVMLVA
FFLCCLLFYF NQRQQNNLRK EREAEREVHN RQLAEALQAA QAASNSKTMF LSNMSHDIRT
PMNAVLGFAS LLAKDAENPE KVREYTKKIM ASGQHLLSLI NDILDVSKIE SGKVVLAIEE
FTLNDLVSSV DAIIRPMANA KEQTFNIEVT NIEHEYLQGD ETRINQILIN LLSNAVKYTP
QGGNIWFRII GLKQRSSQYE HIRIEVEDDG YGMTKEYLKT IFDAFTRAEN STTNKVQGTG
LGMAITKNIV ELMGGTIDVF SEVNQGSLFR VDLELSIPQE QKYKRFWEES GIARVMAVSG
SAEGGKNIQM LMKDVGITVH TAFDREEAMC LIADCSSRQE GYDAVLLDWD TPERNAVRIA
EEIRKILPET VPILFLTAQG PEGVEDALRM KNTGVLSKPF FVSAFQEKIS EMAAEKDGAV
LQEPAEHDNL EGMHFLAAED NEINAEILRE ILSIEGADCE IVENGKLAVE RFEAAAEGTF
DAILMDVQMP VMNGYDATRA IRALKREDAK EIPIIAMTAN AFAEDEKEAL AAGMNIHLAK
PIDIALLRKV IKQCVQRKE
//
