ID A0A101WKX4_9FIRM Unreviewed; 1169 AA.
AC A0A101WKX4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=APF81_12015 {ECO:0000313|EMBL:KUO74981.1};
OS Desulfosporosinus sp. BRH_c37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO74981.1, ECO:0000313|Proteomes:UP000053148};
RN [1] {ECO:0000313|EMBL:KUO74981.1, ECO:0000313|Proteomes:UP000053148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO74981.1};
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 (OCT-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KUO74981.1}.
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DR EMBL; LOEW01000166; KUO74981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WKX4; -.
DR Proteomes; UP000053148; 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; 3.
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; 1.20.120.160; HPT 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; IPR036641; HPT_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; IPR013656; PAS_4.
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; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 9..79
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 81..133
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 134..179
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 221..273
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 274..323
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 349..403
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 432..653
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 672..793
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 819..935
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 980..1073
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 725
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 868
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1019
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1169 AA; 131420 MW; 589E4BF7B84EDA7F CRC64;
MKNSSTDTHE EKYRRLIQTT SEGFWLISAQ FVTMDVNQAL CKMLGYERNE MLGKSIFDYV
DDKNKEIFST SVSKITVQDH RSYEIVLQSK TRQEVYCFFN TTTVRDTSGK IEGAFALITD
ITERKRIEEA LEGSQRQLAD IINFLPDATL VIDTNGKVIA WNLAIEEMTG IKASEMIGKG
NYEYAIPFYG ERRPILVDLV LLPNEIFEKH YNFIRKEKNR LTVEADVPAL RGEKRFVFST
AAPIYNLKGE VEGSIQSIRD LTDRRQAEIA FQESEGRFRT MMEQLPIAMQ VYTTDGILQS
ANKAAEELFD YSAKEFIGKR NVLKDEQVKK IGALPFIEKV LQGETVPAFE SRFDVAASFG
KGRELFLKSR YYPIKNADGN VKNFVILHED ISELKQYQQH LEEMIEKRTL ELKLAKEVAE
AAASSKSEFL ANMSHEIRTP MNAIIGFSGL ALKTDLTPKQ YDYLKKIDTS AKSLLGIIND
ILDFSKIEAG RMEMESIDFR LEDVMNNIVN IISVEAAKKG VELLSTITED VPRALIGDPL
RLGQVLTNLA NNAVKFTETG HILIKAELLN KDEKLCKIKF SVKDTGIGMT RGEIDKLFTA
FSQADSSVTR KYGGTGLGLT ISKRLVQLMN GEISVESSSG KGSIFSFTAE FVRQPEEKEH
SLLTPPDLAG IRVLIVDDSE PAREVLSEQI MSFGFESISV ESGEKAILEL KRAAADKPYD
LVLMDWKMPE LDGIETSKII MKDQRLSHTP LIIMVTAFGR EEVMKRAEKA GINDFLMKPV
NQSLLFDTIM QSFNYNVSST ADSLPRSDMK ITLGMEGAKV LLVEDNLMNQ QVAMEILKEA
SLVVDIANNG QEAVEAVTGS DYDLVLMDVQ MPVMGGYEAT RKLREDGRYG SLPVIAMTAH
AMQGAKEDCL EAGMNDYVSK PINPDQLFSV LTRWLRSHRP DTGIKAKMLT QPNGQDFESN
LPKRLPGIEL ETGLKRLNRN EKLYKRLLLD FSEKYASFTV EIRKALQEKD TDTAERLAHT
LKGVAGNLSI IGVYDLAQGL EEAIAALSAP AIDRLLVELD KELELVTQSL IQLNPVEQKE
LTDIELDDKE PPINMVEIQG ILLELIKLLH EDNLDATECL ETLKKSLGKS MFHNEIQEVD
AYIKNYDFDS AKQSLKRITL GMNIEMGEF
//
