ID A0A1I1PI77_9FIRM Unreviewed; 1142 AA.
AC A0A1I1PI77;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMN02910398_03919 {ECO:0000313|EMBL:SFD05750.1};
OS Butyrivibrio sp. YAB3001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFD05750.1, ECO:0000313|Proteomes:UP000198944};
RN [1] {ECO:0000313|EMBL:SFD05750.1, ECO:0000313|Proteomes:UP000198944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAB3001 {ECO:0000313|EMBL:SFD05750.1,
RC ECO:0000313|Proteomes:UP000198944};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOKR01000031; SFD05750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1PI77; -.
DR STRING; 1520812.SAMN02910398_03919; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000198944; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; 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; 3.30.1180.10; -; 1.
DR Gene3D; 3.40.50.10170; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003797; DegV.
DR InterPro; IPR043168; DegV_C.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00762; DegV; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02645; DegV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 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; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS51482; DEGV; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198944};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 24..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..434
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 467..585
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 952..1049
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1047..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 516
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 991
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1142 AA; 129414 MW; 5383E99A028A39A6 CRC64;
MISRFFMSII ERLKDSSRSF KERVFILLTM VTVLAIALAL IGDIVCGENV VEIVTLVVTI
IIVPVITLVS VMKNNVVLAV RIIVIGLVCV ILPILFYFGG GVEGGGVLWL IFAYLYTGVV
LSGKWKPVLL TVLTFEACIF YATSYFYPDL ISGHPQNVFY IDSLLSVIVI GIVGCLMVWF
EEWLFREENK RAREETSKIE ELVRAQNRFF SSMSHELRTP INSILGLNEI ILRQKDASDE
IIRDANNIQG AGRMLLSLIN DILDLSKIEA GKMDIIPVNY NLGVMVSEIA NMMWMRAEQK
GLEFKIEIDP SIPAEMFGDE VRIKQILVNL LNNAIKYTKE GTVTLHIEKE ELHDNEIRLL
FSVIDTGTGI KQDTLPYLFD AFQRVDEEKN SKIEGTGLGL AIVKQLVDLM DGKITVSSVY
MEGSTFMVSL WQKVTSPDAI GNLNISDYEK NKTRSEFIPE FTAPEVRILI VDDNEMNLAV
ESKLLYDTEM EIDTAINGED ALSMTLNDRY DVILMDHLMP GMDGIKCMQL IRNQTGGLNK
HVPIIVVTAN AGTEDIELYN SSGFDGYILK PVSGKQLEEK LLEYIPEYKV VRSAGTDLNK
VQMNTARGYS KKLPVIVATS SMCDLPEEVI SECGIDILPF SIHVGGKTYY DRYEASTDEV
VYYMKNGLSF DSSAPTVEEF EVFFGQEVKK AHQVIYFTLP PEISKEYENA TEAAKAYGNI
LIFNSDVNSS AMGMLVLFAH RMALQGRNAE KIMDELNYLK TKMSCSFVTS DAGFMMKRGT
VGKGIYSFMK IFDLRPGLCV KNGKLSVTGM YVGELGKCYE KYIDNALPKR IKPDLDVIFV
DYIELRDEEM KSIEARIRKR FAFEHIIFQK ASAVMSLNCG MGAIGLAYAI KGDHPYRFDQ
IFSPVFRDDE EDVIYKEEEP LNTEMMSSVE EPKWYDDIKE IDVQKAIENS GSEETFKGVL
KIFYDSVIPK SKEIESLYNN ENWNDYTIKV HALKSSARIV GATELGDEAE RLEMAGKKSG
LNYIKEHTQS FLQDLMNLRE KLSSIYEDEG SGKRDKKEDK IEKSTKEDKK QEYDNILIRS
AYQTIQRCVE EENISLLKRT LVELEDYDVS DYDRRILDNI KECCNEENYE KISDLLPKDC
GI
//
