ID A0A395YQV3_9CLOT Unreviewed; 970 AA.
AC A0A395YQV3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=DXA13_00615 {ECO:0000313|EMBL:RGZ01845.1};
OS Clostridium sp. AM58-1XD.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2292307 {ECO:0000313|EMBL:RGZ01845.1, ECO:0000313|Proteomes:UP000266320};
RN [1] {ECO:0000313|EMBL:RGZ01845.1, ECO:0000313|Proteomes:UP000266320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM58-1XD {ECO:0000313|EMBL:RGZ01845.1,
RC ECO:0000313|Proteomes:UP000266320};
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:RGZ01845.1}.
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DR EMBL; QSDR01000001; RGZ01845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395YQV3; -.
DR OrthoDB; 9810305at2; -.
DR Proteomes; UP000266320; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
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; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF53850; Periplasmic binding protein-like II; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000266320};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 589..810
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 841..962
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 893
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 970 AA; 108629 MW; 0A9B21072B8E4DB3 CRC64;
MIGLQFLILR QKEKAVVSIR SRKYRFQAVV VFLILTLSLC TYAFSVYGQE IQNEEKENEG
TESRIVKVGF TQVKNFSEKD ENGHYSGLII DYLNEISKYT NWKYEFVECD NDAIVELLAS
GEIDLMGGMF YDDSLRKLYD YPDYNMGYNY GVLFARRDDR SIRDKDIESL QGKRIGVYAN
ATEKIQRLKR YLEFNHIDCG FVYYDKEDMI DETLHYYLES GEVDLLLGND MEADGKFRIA
AEFQAQPYYF ATTKGNKEVL DGLNYALGQI MDCMPDFIEK NYRKHLADSQ SIQISYTQEE
LEFIRQTKEI RVAVVRKFHP FYCMEDEDAH SGIIPDLLNE IEAATGLKFT YVLADSYEEM
LQLVEDGSAD MAGCFIDQEE FAAEKGLALT LPYVSFDNVI VKNKSVTYPS EGLTAAVLNG
RKLPDTVMAD QVMYCENVED GIDAVNRGKA DYMYGISSSL ERAIQSRRIT GVTIFSLNEN
ESEVAFALPR PASVPLLKIM NKALGNLTVE QKEKIENQNA ISAATEPLTL QTLLYSNPIE
VISVLAVFLL LIIVIIALGA RAKIRRTIMA EELRKAEAAS QAKSNFLSKM SHEIRTPMNA
IVGLSSLAAI SGEASPKVQG YLQKIQSSSE YLLSLINDIL DMSRIENDKM SISHEKFDMS
AMLNEVENII RAQAEQKNIE CTFQIELKHN WFVSDSIHLK QVLLNLLANA VKFTSDGGRI
GLEIHERSCS EGTAEISFAV WDNGIGIAPE NQERIFEAFE QTGTSVSKSA GTGLGLAICR
SIVDKMGGEI SIKSALGEGT EFAFQLEIEL CTTEAAEGCG RDEQDREAND PDKTYDFNGI
RVLLAEDNTL NAEIATELLE IQGAIVEVAR NGQEAVHSFA ESKDGYYQLI LMDIQMPIKT
GLEAAKEIRA GVHPQAQTIP IVAMTANSFQ EDVDAAMNAG MNGFVPKPVN IQYLYHVLEN
ILRNDGKGNQ
//
