ID A0A416ENV5_9FIRM Unreviewed; 1131 AA.
AC A0A416ENV5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DWZ56_04865 {ECO:0000313|EMBL:RHP34849.1};
OS Lachnotalea sp. AF33-28.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=2292046 {ECO:0000313|EMBL:RHP34849.1, ECO:0000313|Proteomes:UP000285302};
RN [1] {ECO:0000313|EMBL:RHP34849.1, ECO:0000313|Proteomes:UP000285302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-28 {ECO:0000313|EMBL:RHP34849.1,
RC ECO:0000313|Proteomes:UP000285302};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHP34849.1}.
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DR EMBL; QUEE01000003; RHP34849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416ENV5; -.
DR OrthoDB; 9811620at2; -.
DR Proteomes; UP000285302; 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; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 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; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
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 SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000285302};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 266..317
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 396..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 749..972
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 999..1123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 702..739
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1051
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1131 AA; 127447 MW; 2B029112A7FF1DD0 CRC64;
MFIRIVYLEK ADTKVENKRE EIHNRRLKEA EALASRLMHM HYCEGNAAGV AEYFAPQFTW
VGAGEEQYIA GYDAAKEMFG RFKDAIPKCE ILDEEYDAIE PVPGLYVVSG RMWIATAPEV
KMYLKVHQRV TFVFQEAEKG LLCSHIHCSN PYQEMVGGEF FPEKVGRQSY EFVQERLAKL
EEQTLQQNRQ MDVIMSSIAG GLKISNDDDS YSFAFVSREA AALFGYTVEE FLEVTGGSAV
GAVYPPDLHK ALADCAEAFS GGGLSYSTRY RVRCKDGSLK WIIDSGKKSL DAEGRWMVNS
LYLDITREEE DAQRLREQTQ LLTSIYDTVP CGILRFVYHE DGESELISLN RAALSLLGYD
SMEEGLYDWH RGVLGTVLEE DQDMLRQTYR QLVEVGDRQD RVYRALWHDG SLHWLDGSNM
VVGRTEKGEA IIQRTLIDIT EQKKLQQQLD EEQEMYRVAM EAGNDTMFEY LMDSDVFISY
EPRPGQGVIR RELLHYSQVL LDENFIHPED APRAIDNICN GRGEMFEVRV VTPDSAPGDY
RWHLVSSRLI MKDGRPFRVV GTIRNIHSMK ETLSENSQRL HMNQSALNAI SGVYVSIFYV
NLTEDRYYAV RLPKREDLMS FNRSGSFSGY LCRSVLDYVR QEDWPQVAQV CDRDRLLQWF
PPISGHAEVE FRRNTSDGQP SSWLRLEIHP VSIRNAEART AILTLRNVSD EKRKELERRE
EEKAAKQALE EAYEGARQAN QAKSEFLSRM SHDIRTPMNA ILGMASIAER FLDNKEKVAD
CLTKIRTSGD HLLGLIGEVL DMSKIESGDV GLNETVFSVK DMLITVLDII RTDAQKKEQL
LDWSCCADND LVSGDSMRVQ QILLNLLSNA VKYTQNGGHI SLRAEEKISS RRGVGCFVFT
VEDNGIGIAE EFLDKMFLPF ERAGDARVAA VQGTGLGLAI TNNLVQMMNG TIRVRSRINE
GTCFTVTVFL KLAQEEKPVK EPVLKSQKAN STGFAPGTRI LLVEDNDLNR EIAGELLNMA
GLETACACDG RQAVDLFASN PPGTYSLILM DIQMPVMDGY EAAKAIRLMG AGERPDAADI
PIIALTANAF ADDAYRAAEA GMNEHVAKPI DPDQLLETLH RWLDAAAGGK Q
//
