ID A0A0L6ZAS0_9CLOT Unreviewed; 2027 AA.
AC A0A0L6ZAS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=luxQ_1 {ECO:0000313|EMBL:KOA20074.1};
GN ORFNames=CLHOM_15040 {ECO:0000313|EMBL:KOA20074.1};
OS Clostridium homopropionicum DSM 5847.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA20074.1, ECO:0000313|Proteomes:UP000037043};
RN [1] {ECO:0000313|Proteomes:UP000037043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA Duerre P.;
RT "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT (DSM 5847T).";
RL Submitted (AUG-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:KOA20074.1}.
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DR EMBL; LHUR01000020; KOA20074.1; -; Genomic_DNA.
DR RefSeq; WP_052221068.1; NZ_LHUR01000020.1.
DR STRING; 36844.SAMN04488501_12024; -.
DR PATRIC; fig|1121318.3.peg.1512; -.
DR Proteomes; UP000037043; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14014; STKc_PknB_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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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 Hydrolase {ECO:0000313|EMBL:KOA20074.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOA20074.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037043};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOA20074.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1526..1747
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1773..1891
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1925..2025
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 1485..1526
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1822
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1964
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2027 AA; 231509 MW; 3B94A2133628FD88 CRC64;
MESFTGFKAP TKIFENQDFI FYKSFSEEDQ IPVILKQFTN KNTKEDKFSF FMNELDASKK
LNHDGIVKLL NIISYKVDPI LILEDFGSDI LYNILKNKSF SVKKFLKLAI KLAESVEYLH
NANILHLHIK PDNIFVNWDA EIIKLTGFKG NLATSMTTFD NKKSLGEMQS SYEVAYISPE
QTGRINCKID CRSDLYSLGI ILYEMLTGKR PFESEDPIEI IHFHIAKEPV PVCLLNPEIP
KILSDIIGIL LEKKLEKRYE TSHELKCDLK ECLNRLEFKD EKYKIKEFIP CKRNVCGELF
PDEKIFGRET QIKILMDTFE SVKMDNTSKI IMVSGYSGVG KTTLVNTIGT LIKSSGYIFI
HGKYDQYNNN TPYSSFVQAF DNYFNEILVQ GKEQVALWKD KFIQALDSNA SMITKIFPKL
ELIIGPQKHS ELFMFNEAQS ILHSAFIRFF HAVSKDRPIL LFLDDLQWAD INSIKLLQYL
LNNKENFPIL FVGTYRNNEV DSNHPLWSIL TQLSKSMTSE QIITLKPLTL QEVSQLVGSL
FQHWNQDIES FSSLCFEKSG GNPFFLQQLI KSYKDEGILI YAGKEKKWTI NLDQLGITSF
GNALSDILIR KLKKLNIEAI EALKVAACMH NNFEAVTISN ILDLPYEEVS NALQNSSYEG
FIRLSQSDIY SKDIGNTTDT FCFSHDRVKQ AVYSLINIIQ RSEIHYGIGM YLLEKSGNNI
DENENLFEIT EHLNQAEDIF KEKMEILFLT KLNLASGKRA ASFYAYDRAL EYFKRGIETL
GSEGWLKHYE LTLSLLTEAT TAAYASGQVE LMKKYGNEVL ENGRTLLDKC KIYEIRIEHL
TVENKLKEAV DEARYVLSLF NVNLPVNPTT LDISIRYFKI KFALIGRTFE DLKSMPPMRD
GTMLAIMRIL ASAGLAAYTD SEMVFLIITL NIVEISIKYG NSPLSPASYT AYGHFLCSYL
NKRETGYQFG RLAIDLQNTM KSKAYECKVN LIFEILLRHN KEPLRNTLNS FPENHQKGLH
TGDLNSAGYV IMQHLVYMYL AGLELSTIYK VTLEYKEDLL ITGNRIPISI CFMYLQGIEN
LMEGSKVPWE IQGHYYDEKA ELLAYEEVND KAVTFNIYFN KMVIAYLFGQ YEEAINNLKN
AEVNLKGAIG TFCIPVLNFY SALINLKFMS ISSEKTKKRL YSGKAKYFLK KVKSFYKDAP
ENNENKYYLI KAEEARIYGN YELAIQYFNM SIKSAGKNGF LQEEALGNEL AAKMLYSLGR
SHDASKYAQA GIACYTKWGC PSKAKQLQYT LKRSFMGMEQ HTNVDKFKAT ENFDSHQFLD
LETIIRGSQA ISEEIVLSEL LKKMLSIVLQ NSGARKAFFI METNGELFVE AQGTVMDSSI
ELKKAVPLKE NSEILEKLIN YVVNTRETII LNNTEEIRHF TDDNLSNEKE SLSLLCMPIE
SKRNLVGILY LENDLINGVF TRQHMKILKI FASQLAISIE NAKLYQNLEK MVDERTLELK
LKNNELENAN KKLENADRAK NSFLANMSHE MRTPLNGVIG MASMLQKSRL DGEQKESVDA
IIHSAQSLLA IINDILDFSK IQANKIDLEE QNFNLVHMIQ ELLPAFALKA KEKRINLSCS
VKEGSLEFLK GDPLRIKEII INLLSNAIKF TEKGKVEMEV SSEKIEDTTG VLEITVRDTG
IGISEEKLDY IFQDFTQADS STARRFGGTG LGLSITKKLV EMMNGTIKVK SKLDIGSTFT
CKVYLKLPEA IVVHDTSSGE EEYQSIEKLT GYRILVAEDD EISRKYINSI LKYLSCEVTI
VSDGIGVLEE LKLHKFDCIL MDKNMPNLDG IETTRIIRRD EYITGAHIPI IALTASAIVG
EREKLLSSGM DYYLSKPVNE KELIYTLKSA KKSFVLKKTK KAIKNPSTSQ WIEKDIFLEE
ASLYGEDIMS EILDEFLQGY ALTLQRIKNH IENSNFSDAE KEIHRFASTV SIFQCKSFVD
TLRQMETYAR NQNLENLISS YALVVENIVP LSHELENIKN QLSKKLY
//
