ID F7KFT2_9FIRM Unreviewed; 983 AA.
AC F7KFT2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=HMPREF0994_04711 {ECO:0000313|EMBL:EGN34637.1};
OS Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN34637.1, ECO:0000313|Proteomes:UP000003336};
RN [1] {ECO:0000313|Proteomes:UP000003336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EGN34637.1, ECO:0000313|Proteomes:UP000003336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN34637.1,
RC ECO:0000313|Proteomes:UP000003336};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL Submitted (APR-2013) 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:EGN34637.1}.
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DR EMBL; ACTP02000011; EGN34637.1; -; Genomic_DNA.
DR AlphaFoldDB; F7KFT2; -.
DR STRING; 658086.HMPREF0994_04711; -.
DR PATRIC; fig|658086.3.peg.5143; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_21_9; -.
DR Proteomes; UP000003336; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; 2.
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; 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; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003336};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 393..444
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 606..830
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 861..982
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 913
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 983 AA; 111246 MW; 54E6D605D2333DBB CRC64;
MKNNEVQLRR WFLFAVAAVG ILLGILTFTF VNEVKEQLWE QSVGTIIEST RQGENALNIQ
LREDFSSIIS IKKYLEKLPA DARESVMDIV TEFSKMENGV SLYLQDGTCV PEKDGPDLYM
ADQFLMDYGI VNPHISSSTG VNVFDFYTQV RLADGSINYL VKEYNVAAIA GEFSLSFYNN
AGFSYIINTG GDVLIRSPHP GSNKTVKNIF DMLPAGKNDS RAMEEFRQAL LSGKSGWAVF
AYGDADAVFC YVPMKGFSDW YLLSIIPEKV VSEQTYDILR RTIFFVVAVS LAIIMLALVY
ILQMKRTYHK LRTQADYIDH LYNAVPEGVA LISKDTPFRF IQINHEGLRL LNYPEYASND
ALREKQLREL IHPEDWESTK PCFQEAMEKE QKISYVSRFQ RLDGTYFWAA GIIEKMLDEE
GEPILIATFH DITSERLAQE EEKKEKLLER STLIRAISDT HAVILSVNLT ADTLKTIYVK
PGFLEGLQNY SSYSGLLDFV DERLHPDYRE KFRSRFAAGH IIQAPASHST EVFAQCRILL
ADNEYHWVLL QRINVDNPYT EEKLAIFLAR CIDDQKYEEE QQRQVLQNAL DTARSANEAK
SNFLSNMSHD IRTPMNGIIG MTTIARSHLD DRSRIEDCLD KISLSSSHLL GLINDILDIS
KIESGKLALR EEAFLFSRLV LDAVELIRPQ AEEKQLELTA RIPELEEDTV MGDPLRLRQV
FVNIMSNAVK YTPAGGRIYI DVWQEDGLKL GYGSFIFRCT DTGIGMTEEF LKKIFNPFER
SREGDVEKIA GTGLGMTITK NIVDMMNGDI RIESSPGKGS VFTVTFRLKK EEKTLRAQGD
PLSSEGSGPV RDKTECCRGK RLLLAEDNEL NREIAVEVLK CTEMEIDTAC DGEEAVRMFA
DSAEGYYDII LMDIQMPKLD GYEASREIRG MHRTDAGSIP IVAMTANAFA EDVREALRAG
MNAHVSKPIE VDRLLATLEE LLS
//
