ID F7K6J0_9FIRM Unreviewed; 1421 AA.
AC F7K6J0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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_01498 {ECO:0000313|EMBL:EGN41972.1};
OS Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN41972.1, 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:EGN41972.1, ECO:0000313|Proteomes:UP000003336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN41972.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EGN41972.1}.
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DR EMBL; ACTP02000005; EGN41972.1; -; Genomic_DNA.
DR STRING; 658086.HMPREF0994_01498; -.
DR PATRIC; fig|658086.3.peg.1635; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_21_9; -.
DR Proteomes; UP000003336; 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; 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; 4.
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; 4.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 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; 4.
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; 5.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003336};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 80..132
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 211..262
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 256..332
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 575..626
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1043..1266
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1295..1416
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1347
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1421 AA; 161800 MW; 89FD6AEFC07F5855 CRC64;
MREDFKTTLS SIPCGLCVYR FEGGKISPVY HNSVFYEIMG YTEEHIRLVE KETNFLGVHP
DELGELQMHI QEAIRSNGSM QFTYRLWNDT RGEYRWIHLE GSVKETEEDV KQLYGVYSDV
TGQIQTEKEL SRANEKMQDI INAIPGGVAI YKVSDTFDTV YFSDGVPEMS GYTVEEYREL
IKRDAAAMIY WEDVEMVTAR AREVIRTHEI DSFEFRCRHK DANIVWVRVQ VKWIGEEDGY
PMLHCVFHNI TDLKETQLEM NHLVNSIPGG IASYRVEGQN FIPTYFSDGV TALSGHTREE
YEKMTGNNVL DIIYEQDRER VREAAMNALQ SGEVLDVSYR MRHKNGQLIW IHLNGRRMGP
LAENTGFYAV FTGMSADTRL FQSMVNETAD GIYVIDKENY DLLYVNESRN LFAGGKNCVG
QKCYSALHGQ DGPCNFCTLK DHEPDGEEHE MSADRNGRFY STRFRETDWN GIPAYVKYVR
DITETVTNRK EKERLEQYFQ TVLKNLPGGI AVMRYEEPGR LIPEFLSDGF AAMAGMSLEE
SWELYRNDAM AGVYPEDREY VYQQMDSYVA GGEHREIVYR LRRGDGSYIW VKNNITLIKY
EDGETRIYSV YQDMTKEREA QERIRQQYKD LLLQHYHTQD PNALIIGHCN ITKNQILEII
DHTNSDLLKT FGSAREGFFT GLGSLVVDEE ERQEFYGMYL NKPALEAFRN GIPERQYECF
VQIPRETKGR YVHIKMNLVE EPDSGDVTGI LTVTDITKQT ISDRILHRLS SAGYDFVSDI
DLTCDSYTVL TWNENAGCIP PRQGYYSQWV ERMLEDNVVP KDRERYKEVM DPGTLLERLK
KSSPFTFAYS MTDNRGDVRT KNVTLSVVEP RLGRICLARA DITDSVREQQ GLLRLIAYTF
ELSGFINIGS GGLTLYSRNT VLENLPPYFS ENYGEAIPRF VNRYISEDNR EEAACQFDLK
TMIRRLEEKP NGYDFLVSYR DKNGERYKQI NVMWGDVNHS TICLVRADVT DVLAAERQTK
KALENALELA EEANRAKSDF LSAMSHDIRT PMNAIMGMTA LAVAHMGEPE RVADCLNKIS
VSSRHLLSLI NDILDMSKIE SSQIKLNNMK IYLPDLLDQL SAIMSPQARD AGLQLTISTE
GIKHKYFYGD SLRSNQILIN ILSNAVKYTP EGGTVDFTVE EIPAVNGPDR VRYRFTVSDT
GVGMSEEFLS RIFEPFTRSS GTLRVEGTGL GLSITKGLVE LMGGTISVKS LPHRGSTFCV
ELEGECADGE LENPGEKGGA EFPDAANRKL FAGRRFLIAE DNAINAEILC ELLSIYGAET
AVKTDGAQAL TEFREAAPGT YDAVLMDIQM PEMNGYEATR RIRRLERPDA WEIPVVAMTA
NAFAEDVRAA MDAGMTAHVA KPIDVEVLRE TLKKVLIEKK E
//
