ID R6WT29_9FIRM Unreviewed; 1016 AA.
AC R6WT29;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=BN605_00607 {ECO:0000313|EMBL:CDD07136.1};
OS Dorea sp. CAG:317.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1262873 {ECO:0000313|EMBL:CDD07136.1, ECO:0000313|Proteomes:UP000018262};
RN [1] {ECO:0000313|EMBL:CDD07136.1, ECO:0000313|Proteomes:UP000018262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:317 {ECO:0000313|Proteomes:UP000018262};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD07136.1}.
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DR EMBL; CBGJ010000052; CDD07136.1; -; Genomic_DNA.
DR AlphaFoldDB; R6WT29; -.
DR STRING; 1262873.BN605_00607; -.
DR Proteomes; UP000018262; 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; cd17574; REC_OmpR; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 2.
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:UP000018262};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 439..654
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..802
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 913..1013
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 735
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1016 AA; 115056 MW; 5C16DD5B6E494D4B CRC64;
MKTINKHAIK KITPFHIWII SLLLIPVIFY FFIVTPDTAK KATTGALNAS YIENHFPVAL
NGEWEYYDNQ FLFPSDFSYN RKSTSVPEYR NLPGQLSSTY GYGTYRLTFS FLGTSDLYSL
RLTSIPGAAR IYIDGNLLSD IGFTSSLKES SETIKDNQYV VFPLDIMRQT HEIIIQVSNF
SNYHSGMSSP IYFGTQIEGY RLSSQFKFAE SVGLMSVGVL AILLIFLLIF KIQMKGTFYL
LIFTLSFSFH LIYSSTDLLT QPVHSSTYFI MTKIHVFLYC IMGLCMILSA MQIDHKTEKS
QYIRKIYLYC VPVLFLAIFF SSDRFFFYAK TFTIIYLIIT FLHTMLLLLR RILHNSHSAL
MLHLSFIFFI SYFILLYFNS QGMVSAISYN GSYTFLLIAY VTSQLAYVAL QVSKIYTGNT
RLAHRMVATN KLKSEFISAT SHELRTPLHG IINIIESTGT KLDNPNIAKE QLQLGLMLAR
KMNRVLNDLY GFYSSAERKN ATLKPVNLDT EVNAVIELFH YTSTNSRLIL KNNLAQDALW
VLADESKLWE ILNNLIGNSI KYTESGTITI SSKKENEKVF ISVMDTGIGM PSKDINRIFD
KSVRLDSAVE KSTGIGYGLY LTQKLIQQMD GTIFVDWTSP GKGTCITFSL NSCEPDSDFD
PNVIISPEQY DASNNYLEDF SGSSASILVI DDNKDNLSII RTIFEDCSFD IDCIQCPKEA
LSLLEKSSYD IIILDVLMPE MSGFELCQLI RKRYSHFELP VLLLTACDSS EEILTGFWSG
ANDYVVKPAD RIELRTRVFS LITLKQSVKS ALDNELLFLQ AQIRPHFLYN AFNTISAIAL
SDGLKASELI DDLAIYLRGC FGTNVNQGLV SIKTELGIVN SYAHIEQARF GERLQFTSII
NTKKDFSLPP LTIQPLVENA IRHATLDSYQ KIDVKLTITE NENCIQITVQ DNGKGIEPTK
IADLLDEEKI SHQGGIGLKN VNRRLRLHYG VPLDIQTIPE KGTRILIQIP LTPDNK
//
