ID R9N0K7_9FIRM Unreviewed; 848 AA.
AC R9N0K7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=C819_01213 {ECO:0000313|EMBL:EOS76829.1};
OS Lachnospiraceae bacterium 10-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235800 {ECO:0000313|EMBL:EOS76829.1, ECO:0000313|Proteomes:UP000014134};
RN [1] {ECO:0000313|EMBL:EOS76829.1, ECO:0000313|Proteomes:UP000014134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1 {ECO:0000313|EMBL:EOS76829.1,
RC ECO:0000313|Proteomes:UP000014134};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 10-01.";
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:EOS76829.1}.
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DR EMBL; ASTF01000011; EOS76829.1; -; Genomic_DNA.
DR AlphaFoldDB; R9N0K7; -.
DR STRING; 1235800.C819_01213; -.
DR PATRIC; fig|1235800.3.peg.1301; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_21_9; -.
DR Proteomes; UP000014134; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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:UP000014134};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..571
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 585..705
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 726..846
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 639
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 778
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 848 AA; 96035 MW; 5D9BE956C0C7ACB2 CRC64;
MKNKTIRLLT ISLIAIAFVC VMVFTFLASF LGRKNTQMIS EIGTIYMAGM NERIEMHFKS
TIDTQLSQLE SIVEEIPEEN ISDYALMEED LKYSAEGRNF QYLALYSGDG DFEMITGEQV
MLADPEPFWE SMKKGDKKIA VGVDASANDI VLFGIRAELP MADGRKSIAL VAGIPDEYIV
RVLALEENDS LVYSHVIRRD GSFVIKSIAT EKNSYFEQVR AIVDEEAGKS AETYVEELQS
AMRERKRYST VLHMEGSRSH LYCTSLPNSE WYLVTVMPYG AMDETVSHFS AIQVTSIFIG
SGIILFGLLV VFILYLNLSR RQMEELEKAR EEAVHATRAK SEFLSNMSHD IRTPMNAIVG
MTAIAVANID DKKQIQNCLK KITLSSKHLL GLINDVLDMS KIESGKLTLH IEQISLREVM
DSIVNIVQPQ IKEKKQHFSV HIRNVEAEDV YCDSVRLNQV LLNFLSNAIK FTPEGGYIEI
SLYEEPSPIG DTYVRVHIKV KDNGIGMSDE FKKTIFEAFT REDSKRVQKT EGTGLGMAIT
KYILDAMEGT VEVNSKQGEG TEFHVILDLE KVLVQEEEMI LPDWHMLVVD DDEQLCESVI
HALKDIGINA EWTLDGEAAV ELVKERHKQQ NDFQIILLDW KLPGMDGIET ARSIRTQMGG
DIPILLISAY DWNEIEHEAR EAGITGFISK PLFKSTLFYG LRQFAETDNE IETQLSEKEI
DLTGRKILLA EDNDLNWEIA EALLTERGLE LEWAENGQIC VDKFKRSPVG FYDAVLMDIR
MPVMTGHEAA REIRALDRED ADIPIIAMTA DAFEEDIKRC MESGMNAHVA KPIDIREVER
QLDKFIKK
//
