ID A0A0F2N8H0_9FIRM Unreviewed; 1042 AA.
AC A0A0F2N8H0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=VR68_10750 {ECO:0000313|EMBL:KJR98337.1};
OS Peptococcaceae bacterium BRH_c4a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJR98337.1, ECO:0000313|Proteomes:UP000033439};
RN [1] {ECO:0000313|EMBL:KJR98337.1, ECO:0000313|Proteomes:UP000033439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJR98337.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJR98337.1}.
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DR EMBL; LADN01000068; KJR98337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2N8H0; -.
DR STRING; 1629716.VR68_10750; -.
DR PATRIC; fig|1629716.3.peg.3622; -.
DR Proteomes; UP000033439; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 447..666
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 701..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 751
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1042 AA; 116997 MW; 53088A07570B7B28 CRC64;
MLLKSKKVII LLLIIATAIM MVFYFLQKTP SADLPVAKNG FIDLSDWNFD KDGNIKLDGE
WEFYWGSLLT PDDFATAKPN SSIYPDGYIK VPSPWKGKIG NAQLSDNGVA TYRLKVRLGS
VNTMYGIKTT SIRMSNKIFI DGFEVGKRGN PAMSYKDGYI MANTPYVTFF HPKSNELEVI
VQVADFDYRA GGIVQSIYLG KRTDIFVMAG RFNFFNGFVA ACLLITGIYY LFVYLGRRKD
LSLMYYSAYA ITFSFFELAY GEKILNQMFP DIPEVIITKV LNILLYASII FICLFIKSIT
GKLLPDWFTR TVVIVMGGYI VLLSVLPIKM SLSVQDIFLL FGMTVYVFIL AFLVFAVVQE
QYGNLGRNGF IQLIIALTCV LIYFADGVIY INNMKNDNYI GYAALLLFIA MISSMLSQQY
NNAYNTIERM SVKLLESDRL KDEFLVNTSH ELKTPLHGII NITRSVLESA SGTIAEKQKE
SLNFVVTIAK RLSSLINDII DFQNLKNHTL HMDIRVFDLH APVQVVLEVL KYMRAEKELS
LVNRIPPGTF FVRADENRLR QIIYNLVGNA LKYTERGKVE IMAWADENRI VVSVEDTGMG
IPEASQESIF LPFDHTGNTG ASEYRSSGLG LPISRRLAEH MGGKLLLDWS VPGKGSRFIF
TLPSDSGKEA ADKSAAAAAY LQYGADTEEA AQKSAHSRFY TILLVDDEVS NIRVLTDMFR
EEDYETVVAY NGGQALEMIR QNRNISLVLL DVMMPGMSGF EVCRKIREEY SLSDLPVLLL
TVRNTPQDIE TGFKAGANDF VAKPFNAREL RARVSTLIML RRSVGEAVAN EMAFLQSQIK
PHFLYNALST IMNLCYTDGE KAGNLLASLS EYLKKSFDID STACSSSLES ELELTKAYTD
IEQARFRERL KMVYRIDSSL PELRILPLTI QPLVENAVRH GIMPRESGGT VTLSVQKAGE
FVEVCVEDDG VGFTDAEAVL KKEAGNKKQR NGVGLSNIQR RLVNSYGSGL WVNSSEETGT
RVTFHIPLDM KDRNHEHENN GE
//
