GenomeNet

Database: UniProt
Entry: R0ACW2_9FIRM
LinkDB: R0ACW2_9FIRM
Original site: R0ACW2_9FIRM 
ID   R0ACW2_9FIRM            Unreviewed;      1122 AA.
AC   R0ACW2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=HMPREF1085_02627 {ECO:0000313|EMBL:ENZ49921.1};
OS   Enterocloster bolteae 90A9.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ49921.1, ECO:0000313|Proteomes:UP000013126};
RN   [1] {ECO:0000313|EMBL:ENZ49921.1, ECO:0000313|Proteomes:UP000013126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90A9 {ECO:0000313|EMBL:ENZ49921.1,
RC   ECO:0000313|Proteomes:UP000013126};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium bolteae 90A9.";
RL   Submitted (JAN-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:ENZ49921.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGYH01000006; ENZ49921.1; -; Genomic_DNA.
DR   RefSeq; WP_002575806.1; NZ_KB851182.1.
DR   AlphaFoldDB; R0ACW2; -.
DR   PATRIC; fig|997894.4.peg.2770; -.
DR   HOGENOM; CLU_000445_114_21_9; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000013126; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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   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; IPR035965; PAS-like_dom_sf.
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: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; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          499..723
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          875..997
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1004..1122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         928
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1056
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1122 AA;  123848 MW;  5E05532102FD01B1 CRC64;
     MKQIRKKHKF SLPITITVCI ALAIVFYLSL SYFLEGYRRD IYDRIINSNI SALKETTSTL
     ISKTTEGFDH CRHEIRVLGI GMSEELKENG FDSIDGLSNG DRSYLRDFNK VSVFDYCVLL
     NESGRGVYSQ GDSVKPINLY SSQAYVDCLN SPDGEAISFI SDPFSASGQD VVAFSCRAGS
     VILIGIYSQE SFRALYDSTA FGDNASYMIT TDSGLILSRT HVNRELGETL NLFTYFEENP
     LNAEFFKPDA QGGTEYERVL SEFRNDKGGS AEIYFGDSRY ELVYAPIPRT GWEFISCVSY
     DHITADAAQI NQETIQLTMF IIVLMLGMFL VIVIMLVFVV RANASREAVR RDRIFTLMTH
     YVPNVIVIGD SESGAIEYAS RNTEQVLGIE DAFGNAIEEK FLSCISGSDR QAVLDLMSRI
     REGECVSGSL KLHFTRPDTQ RDIVLSLNAY LIAEQDSSQR FITLTLEDIT EREQSRRRLE
     EALESEARAN AAKSTFLASM SHDIRTPLNA VIGLTNLALY SPEDSKKVTE CLQKIANSSQ
     LLLGLINDVL DMSKIESGKM QLAETEFELG EWLSGVVTVT QSQTGVRSQH FDVNVWNITH
     ELLCGDTVRL GQVLTNVLGN AVKFTPKDGE IYLDITEVPS QDPSFASFVF RVSDTGVGMS
     REYMGRIFEM FSRDQNSYKQ GIQGTGLGMA ITKRIVDLMG GTIRVESEPG KGTTFTIGLS
     IRLSSRHVPL AAGCAMLVIG EPGSEEKCRD AVEKLEEIGV DAAWETDYQA AVSLAAQKRA
     AGRPFSMVFL PYKMLRFDRT LTGEQLKRDL GGDTLLLLGL KPDEQELFEE IKQKGFKYTI
     SLPLFRMSLY RKITGMLGQG ESISGGLAGE LKGVRLLVVE DNAVNLEIAV EMLSGLMGAA
     VDTARNGEEG CTRFLDAPED TYDVILMDLQ MPVLGGLDAA RRIRESIHPQ AASIPIIALT
     ANAFEEDRRE ALEAGMNGFV PKPIDFAVLA KEIGRVRREG RSLRLLLAED NELNREIAAE
     LIRADGQQVD AVENGRQALE AYLNAPDGTY DAILLDLRMP VMDGFEAAAA IRGSQRKSAG
     TIPVFACTSS SEDEVRSEAA RAGFGAVLTK PINMEQLRGL LG
//
DBGET integrated database retrieval system