ID R5ZJA6_9FIRM Unreviewed; 989 AA.
AC R5ZJA6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=BN504_00503 {ECO:0000313|EMBL:CDA28967.1};
OS Eubacterium sp. CAG:156.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262880 {ECO:0000313|EMBL:CDA28967.1, ECO:0000313|Proteomes:UP000018124};
RN [1] {ECO:0000313|EMBL:CDA28967.1, ECO:0000313|Proteomes:UP000018124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:156 {ECO:0000313|Proteomes:UP000018124};
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:CDA28967.1}.
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DR EMBL; CBBN010000064; CDA28967.1; -; Genomic_DNA.
DR AlphaFoldDB; R5ZJA6; -.
DR STRING; 1262880.BN504_00503; -.
DR Proteomes; UP000018124; 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; 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; 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:UP000018124};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 486..710
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 725..845
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 867..989
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 779
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 919
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 989 AA; 111481 MW; 2928134BF6EBE958 CRC64;
MKLENSKNSH LGRMMGSLSL GVMIFAVALA VLMNIQTTRK RVSEQTAQYI KISTMQNEQI
IDRLLVDAKE SIKSIGKLFG QIIDENGNVT AHDIESLNQN VSFESLIYVN KHGIGIDQNN
IEYAFADATA YYDALKGDTV IALNPLGNSD MQNRICFFAP VEKDGEIAGV LVGNFDDATL
KKFMNTKLFG YTSTAFICSE SGEIVANSVG ILQRTTLTSY LKEHNLMDDN GIAELRNSLK
NKNQYAFEIH GKNYESSAYM MRLENSGLIL VQAFPVEATN KLNATANKDS WRLVTILAVF
FIIYLIGTVV FNVKKQRNIM NEKESVENIV TAITQMFDRF ILVDLDEDKY EYIIEDENKK
LPGIGFEGSY GDILQNIFSK CFKNDEKHTS VDTMLQREKL IEQLDFGKDS FSLEYSEEFD
TDNEFRWTNL AVLCVERRRG VPTKVLMASQ DETELKKKEV RDQEALREAY QAAENASNAK
SDFLSKMSHD IRTPMNAIIG MTALAGSYID DKDRMLECLK KITSSSKLLL GLINEVLDMS
RIESGNIKLV DEDIELSVLL EDVLELVKGD VKNKNLDLNV SIENMKHEKV IGDSIRIQKI
FTNIISNSIK YTPNGGKISI TVNEKPTHSK STSCFEFIFE DTGIGMSKEF VKKIFVPFER
AEDSRIDKIQ GTGLGMAIVN NIIHMMGGEI QVESEINKGS RFTVTMVLKL QDDKEETDKE
LINLKVLVVD DEKVVCDSTC KVLNSIGMNS EGVTTGKEAV TRVVEEHEKN DDFYAAIIDW
NMPEMNGIET TKEIRKAVGK DVPIIIMSAY DWSDIEEEAK AAGVNAFISK PLFKSRLTTT
FKQLLNNNQE EENPLSVLKN EDYSNRRALV VEDNELNAEI MREMLNMTGI KVDRAENGKV
AVEKLESEPE NYYDIVFMDI QMPIMNGYQA AEAIRQMDQR KDVHTIPIIA VTANAFVEDI
LTAKAAGMNE HIAKPVDIKE LDEILQKWL
//
