ID A6TPW2_ALKMQ Unreviewed; 773 AA.
AC A6TPW2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Amet_2069 {ECO:0000313|EMBL:ABR48230.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48230.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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};
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DR EMBL; CP000724; ABR48230.1; -; Genomic_DNA.
DR RefSeq; WP_012063210.1; NC_009633.1.
DR AlphaFoldDB; A6TPW2; -.
DR STRING; 293826.Amet_2069; -.
DR KEGG; amt:Amet_2069; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_114_15_9; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000001572; Chromosome.
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; 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; 3.30.450.20; 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; 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; 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; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 2.
DR SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABR48230.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW Transferase {ECO:0000313|EMBL:ABR48230.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 9..79
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 127..197
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 200..252
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 253..325
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 327..380
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 405..626
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 654..771
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 371..405
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 703
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 773 AA; 88928 MW; DC03AD784D58D79F CRC64;
MDDMKKEEVN TNYKNVLEDL MDIILIVDKN GKIVYGNKRA VETYGYTYEE LVNLSVFDLR
NQDIEEPVQE QLKQALLRGI EFKTYHYKKN GTKFPVEVRS RYSGEQSKGN VVSIIRDISH
IDKIAKDAEM FSVSLDILDD AIVTFTKDLK VSLWSKAAEE KLGYTKEEIV GQNIKILVPN
EKIKEFENEI FEVRKGNVVE RLETIRLHKN GNAIDVSISV SPFYDPDGVL IGVLGVYKDI
SQRKELAKQL KRNEERWRYA LEGGRFGIWD WDIENNKIFS ADLWKEILGY NEGELNDTYE
DWMSKVHPED FPYVKDKLNK HSRGEKYIDE FRMKCKDNTY KYLRAKGQII EWREDGNPLR
MMGTLEDITD RKIIEEELKE KYKQLELLKE EAENANKAKS QFLANMSHEI RTPMNGIFGV
VQLLESTDVG AEQNKYINML KESTHTLAGI INDILDISKI ESGTFKLNNE PFNLTEMISS
IYHGLLVDGN AKGLEVGYYL DPNINPQVIG DELKLKQILT NLISNAVKYT EQGFVSFRVN
RISFDEHTEK IQFNVKDSGI GIKDGFKEKI FEDFSQEDSS TRKKYQGTGL GLAISKNLAL
LMQGDISFES KLGEGSIFTF TCELQKSRTE DVNTKNHDIV KEKVEYSNQN SNKVILCVED
NIMNQEVMES IVTKKGYQYL AAYNAKEALD ILENKKVHLI LMDIQLPDLN GFEITKSIRM
AKGPMKDVPI IAVTAYVDHK IENKCIQAGI NDYMPKPLDL EKLYEMLESY LEG
//
