ID A0A1M6W739_9FIRM Unreviewed; 1264 AA.
AC A0A1M6W739;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN02745123_03514 {ECO:0000313|EMBL:SHK89449.1};
OS Desulforamulus aeronauticus DSM 10349.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121421 {ECO:0000313|EMBL:SHK89449.1, ECO:0000313|Proteomes:UP000183997};
RN [1] {ECO:0000313|EMBL:SHK89449.1, ECO:0000313|Proteomes:UP000183997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10349 {ECO:0000313|EMBL:SHK89449.1,
RC ECO:0000313|Proteomes:UP000183997};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAR01000028; SHK89449.1; -; Genomic_DNA.
DR RefSeq; WP_072916974.1; NZ_FRAR01000028.1.
DR AlphaFoldDB; A0A1M6W739; -.
DR STRING; 1121421.SAMN02745123_03514; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000183997; 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; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; 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; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 164..208
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 237..288
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 300..329
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 337..399
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 407..454
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 546..769
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 789..902
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 911..1033
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1048..1163
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1173..1264
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 392..421
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 838
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 961
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1096
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1212
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1264 AA; 143135 MW; EBF78152DFF1A45D CRC64;
MRSKVVELLT CNEEVIYQKI IKYAKMGGFT RSSSTRMEDW RLSVRQLIHS LVIFLKESEQ
YKIQVDMDLA NHPITFLGIK SARLHRARGI TLKMFISLFK YYQRAYLEFI RESTLAEEEK
SDALNAVEYF FDLYEIGFCS EWVGEGPESR LIELQVANQQ LTNERNKLRT IFESMTECVF
VVNSQMEIIE INEAAAAYFE VNPEDVIGVH CSNLMGCQCT KEECQLYQAM ITGGCYKDVE
VEVNTRRGRR QLLTSGSFLH DISGEYTGGV QVFEDVTERN LMQQNLRLHM QANNSSIECV
TIFNESAQLT YANAAAVELF GRSEQELIGL GLEEIYYQNE KLLLSLVRGE SWRGEITQTG
CTLNVHANPI RLTSGKISGF YVAAKDITNH KMTQLKLQQA REETEREAAK LRAIISIMKA
AIALVDANDV VTEVNEQCAA LAGMTREDII GKKLWDIHKG ETLVKVRSII DEYRINPNHP
PRTITRRMGE MDVIMNIQPV YRDHTYDGIL LMVVDVTEVA AAKRQAEQAR VAAEKANQAK
SEFLANMSHE IRTPMNGILG FAEVLMHQQL DAQQEESVKI IQQCGEQLME LINDILDLSK
IESGKFTLEE TDFSLRKLIY EAISVVEPKL LEKDVEMKIN IEPNLPDDFK GDPTRIRQIL
SNLLSNAAKF THQGFVKLTV SHNSIGNEDR RFNLKFMVED TGIGITKEKL TLIFEAFTQA
DGSTTRKFGG TGLGLTISKN LAQLMDGEMT VESEENQGAT FVFTIPLDQV EVQQVVQSVE
EKGEQSSGVV LVVEDDWATK QLIANYLEKA GYTVITTDQG KQSLTMVKIY RPDIIILDIL
LPDLNGWEIL QKIKLQEGCQ DIPIIVCSIL PEKERAFSLG AVDFLEKPVS EKTLIERLRR
LIGQRNTVEN NVVLVDDDHN VLQFLSCVLG EAGYQTHTFI KAEEALTYIL NGGLVQAIIL
DLMMPGMDGF EFLDKVRENP QFKNIPVLIN TVKDLTPEDY QKLNDKYEKI LNKRVAQPGV
LLEELASLVR SGVANSELSK KATETKLTIL LVEDNRFNQK LMRQLLSEKY QVMVAENGQQ
AIDLLEKNKF DLLLMDMQMP IMDGYEATRR IRQMSQFHDL PIIALTAHAM KGDYEKCIEA
GCNDYLAKPV KRDTLLKTIK QYLKESNKKI RSRDTGIEAL VPWYLQDLSE EMDKLKYAAK
VNDFTTVQYI GHGLKGSGGA YGFPEFSALG ASIEKAATNK DSDLVKSLVA ELREFYTKIL
EEEL
//
