ID C0EED5_9FIRM Unreviewed; 1192 AA.
AC C0EED5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, 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=CLOSTMETH_02215 {ECO:0000313|EMBL:EEG30183.1};
OS [Clostridium] methylpentosum DSM 5476.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG30183.1, ECO:0000313|Proteomes:UP000003340};
RN [1] {ECO:0000313|EMBL:EEG30183.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30183.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG30183.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30183.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476).";
RL Submitted (FEB-2009) 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:EEG30183.1}.
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DR EMBL; ACEC01000068; EEG30183.1; -; Genomic_DNA.
DR AlphaFoldDB; C0EED5; -.
DR STRING; 537013.CLOSTMETH_02215; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR HOGENOM; CLU_000445_114_21_9; -.
DR Proteomes; UP000003340; 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; 2.
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; IPR032710; NTF2-like_dom_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 InterPro; IPR037401; SnoaL-like.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF13474; SnoaL_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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:UP000003340};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 172..220
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 223..274
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 268..342
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 345..396
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 684..907
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 927..1047
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1066..1187
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 981
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1118
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1192 AA; 135087 MW; 4D5C52421CF8EB08 CRC64;
MNGSIDAKQT AKDFCLAWFE ERNLEKTASF LTEDISFVGT GIGESATGLP EMAAYIRQDI
SEIPEPFRMK WTLQHEQPFA EGITSLVVEM TLINSYYTWH LRACFVCRKE RRKWLICSVQ
ISEPSSNQRG NEHYPQSLVL ENVLKQRQEL LNNSIAGGMM GGYIAPDFPF YFINRRMLDY
LGYASEEEFV ADIHGFISNC MHPDDRDAVD TAVSEQLKEK GEYIVEYRMK KKDGSYIWVH
DVGRRMTAEN GRPAISSVCI DITLQKQAQN EVLHIYNNIP GAVFRCRFDD DFSVIEANDG
LFEFLGYTRE EFAEMGNRMS AVIYPEDLEV MAQRLNEQLE SGNTIQNENR LICKSGVVKW
ISIKAQLFQE EDGERYFYCV FVDISDEKQL QERVKELYEE ELAYFAELSS STGSIQGRIN
VTQDRVETYL STSEVAIASV GTSYLETVES LATSAVDPAY GEKIRCQLDR EKVLGDYAAG
KVDYHFEFLR RRNDDGAFWG STNLRTCLNP ETGDIIIFFY TFDITEQKLQ EILLSKITQL
GYDIIIEIDL QQGTHRLVSF QSERTDSISP RGEFQKEIRA IAEEHMDQAS RQEYFQKLDF
DYMKKHLEKE DSYTFVVEIK GEDGSMRVKR FQVFWIDRDL ERVCIARADV TDVVRQEQRQ
KEELAAALVA AEQANAAKSD FLSRMSHEIR TPMNAIIGMS TIAAQSIGDD EQVEDCISKI
GISSRFLLSL INDILDMSRI ESGKLLLKSD KIPIEEFLSG ISSICYAQAA AKGVEYECIV
DPVLDDYYIG DTMKLQQILI NILSNAIKFT GEGGKVTFSA SQRRKTKNDA ELRFIINDTG
VGMSEEFLPH IFEPFSQEST GTTALYGGTG LGLAISKNIV DLMDGKITVR SIKGIGTEFT
VDVKLGITEE GKLRHKKKAV HNFSHLKTLV VDDDVAVCES AVVLLKDMGV KAEWVDSGHK
AIDRVQHLWD ENRYFDMVLI DWKMPGMDGI ETARRIRRIV GSDITIIIMT AYDWAFIEHE
AKLAGVNLLM SKPMFKSSLI SAFSKALGEK EDQLQQTQEY DFTGRRVLLV EDNSINTEVA
VMLLESKGFV VDTAENGLRA LELFSKSKEG EYDAILMDIR MPLMDGLTAA TNIRHLSNAD
AKTVPIIAMT ANAFDDDIEK SKIAGMNAHL AKPIEPERLY QTLVHFIFGK ED
//
