ID A0A101WPW9_9FIRM Unreviewed; 924 AA.
AC A0A101WPW9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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_01050 {ECO:0000313|EMBL:KUO77051.1};
OS Desulfosporosinus sp. BRH_c37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO77051.1, ECO:0000313|Proteomes:UP000053148};
RN [1] {ECO:0000313|EMBL:KUO77051.1, ECO:0000313|Proteomes:UP000053148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO77051.1};
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 -!- 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:KUO77051.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOEW01000113; KUO77051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WPW9; -.
DR Proteomes; UP000053148; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19411; MCP2201-like_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR047347; YvaQ-like_sensor.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUO77051.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW 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 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 515..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 805..922
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 439..505
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 855
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 924 AA; 105041 MW; 416552A0C0F78810 CRC64;
MKLNTKLYIC FSSFLLLIII IAVFALNMLN QFKNDMNVVV VDRYEEVRLG INFRYEINNI
SRVERDLILF DKDKDSINKS ILEIEQSREN SLIALDCLDK IANRQEVRVL LPKLKLTNNS
FIEFQKEFET LVLAGRKNEA TQLILTNGIK LRDQMYQMIN ELVGSQERLM RDTLEQTNSL
YRQAIKISIT LIILFLLLGI GVIYITIRNI TDNIKKVRGV INSISSFEST DNLPRINITS
RDEIGDIAKA FNEMITVLEQ HIYHESESTQ ALKDLHWLQS KVSETHASYH GVQDVNSFSS
LTINWICQIV GASYGNFYVR SNKKETVKLI NMASYAGKGQ AFGIAELSPG EGLVGQCFLE
NRIINLTDAP NQYIEITTGF GKITPKHIKI LPVEFEKKVV AVIELASRSE FNPLEREFLE
QVRWNIGIIL NRIEKHAQVQ KLLAESQALT EELQTQSEEL QTQQEELKTF HENLEEQYKE
SELKNIQLLQ AKVNLEEQAH QLESNSRYKS EFLSNMSHEL RTPLNSLLIL ARMLWEDNAG
NLSVKQVEYA KTIWSSGNDL LKLINDILDL SKIEAGIVYF NPEQISLFEL KEELEKQFYP
IAREKELDLL IQVDSDLPDN LITERQYLKQ ILTNLLSNAL KFTNQGYVKM NIQRASKVLS
QDRLSEMENE NTLFAFCVSD TGIGIAKDKK ELIFEAFQQV DGTSSRKYGG TGLGLSICRE
LATLLGGFIE VKSIEGTGST FTLILPSNIV KKTFVASDTK GLFGEAAVGL DFSTNLNSVN
TPNKKIDVEK VTQNILAAGD LTGRIVLVVD DDMRNIFAVS VALESLKIKV LFAENGREAL
EQLQENIDLD LILMDIMMPE MDGYETIKLI RQIQEYKDIP IIAITAKAMK GDREKCLEAG
ASDYISKPLD IVTLISLIRV WLYR
//
