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Database: UniProt
Entry: R5QFD9_9FIRM
LinkDB: R5QFD9_9FIRM
Original site: R5QFD9_9FIRM 
ID   R5QFD9_9FIRM            Unreviewed;       831 AA.
AC   R5QFD9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=BN766_00844 {ECO:0000313|EMBL:CCZ19827.1};
OS   Candidatus Apopatosoma intestinale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Apopatosoma.
OX   NCBI_TaxID=1262966 {ECO:0000313|EMBL:CCZ19827.1, ECO:0000313|Proteomes:UP000018243};
RN   [1] {ECO:0000313|EMBL:CCZ19827.1, ECO:0000313|Proteomes:UP000018243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:724 {ECO:0000313|Proteomes:UP000018243};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ19827.1}.
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DR   EMBL; CAZP010000034; CCZ19827.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QFD9; -.
DR   STRING; 1262966.BN766_00844; -.
DR   Proteomes; UP000018243; 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; 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; -; 1.
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; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CCZ19827.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000018243};
KW   Transferase {ECO:0000313|EMBL:CCZ19827.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        267..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          453..681
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          702..823
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         754
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   831 AA;  93472 MW;  665338718E3E1557 CRC64;
     MMLGTLFFSI EYSRRKAQKT MDRNISDLKK QINDYNEFLA ADEVKSLIRL TEKAESLSEA
     LAMLDDGARQ EYIERIYDSQ RLSCILVLDE NLNPDNFMRT VKCNGTADEC YESWIAELQS
     PAIKAISDHP KKVYSARIRH GGDNYDIAAV ARTDAKGIIF CASRQADKKL ELHYSPVRNL
     LARNETRLDG TLCIAEDGRI IATNLDGAYA GADEIPELTA LKERKAGNEL TMIVSGGDVF
     YGGIVKCRNY DIYAFYPAGA IYSPCRAIML FAFSVYVMIV FIIGFFHSKA RAERAREINR
     QYETIQAISH VYSLTALIDL KANHYELLKY PPDLSNVAKD GTLDTRFCKE IIGYVDERFR
     EGYRDFLNTE TMTERLAEAE YAEYEYQNRN GDWINDKLIV REKDKEGRVD SVILARSSIN
     EQKKAELEYQ AKLETAVRNE QTANQSKTDF LRRMSHDIRT PINVILGMLE IANRNPTDTE
     LLASCRSKTQ TAAEYLLELV NDILTLNRAG VRNSDDIPMT EEFRLQEEVR KLYLIAAETA
     KRYDGVILEP FRISGEDKPL VGEPLYLRQI MINIIANAIR YSKNGGTVRC SVSQNPAQNR
     DGYAEVRFIC EDNGIGMSKE FQKRMFEPFA QESAVSVSHF GGVGLGLSIV QKLVDRLNGT
     IEVDSEQGRG TRFEVKIFYP YANTHDEAET HTYANASLAG LTVLIVEDNE LNMEIAGYMA
     AEAGASVVRA FDGRQAVEKF AASAVGEINV ILTDVIMPEM DGLEETRRIR ALDRPDAKTV
     PIIAMTANLF EDDIREYTDA GMTGVLPKPL NMSQMVETVA KQTAKGGKNN G
//
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