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Database: UniProt
Entry: C0C5U9_9FIRM
LinkDB: C0C5U9_9FIRM
Original site: C0C5U9_9FIRM 
ID   C0C5U9_9FIRM            Unreviewed;       976 AA.
AC   C0C5U9;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
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=CLOHYLEM_07486 {ECO:0000313|EMBL:EEG72483.1};
OS   [Clostridium] hylemonae DSM 15053.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG72483.1, ECO:0000313|Proteomes:UP000004893};
RN   [1] {ECO:0000313|EMBL:EEG72483.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72483.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG72483.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72483.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) 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:EEG72483.1}.
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DR   EMBL; ABYI02000041; EEG72483.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0C5U9; -.
DR   STRING; 553973.CLOHYLEM_07486; -.
DR   eggNOG; COG0642; Bacteria.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_000445_114_9_9; -.
DR   Proteomes; UP000004893; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; 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; 3.40.190.10; Periplasmic binding protein-like II; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00497; SBP_bac_3; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00062; PBPb; 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; SSF53850; Periplasmic binding protein-like II; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEG72483.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEG72483.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        43..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        549..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          599..820
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          844..965
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         896
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   976 AA;  109121 MW;  CD0C782711331124 CRC64;
     MCEAAETGQF MWQNSPRHGK IVTGDFKKEF CMKNRSRLEI KKCGVVLLLL AAALTAVLVP
     CAGARAKEPQ SGKVLKVAFA QVPGFTETDK NGNRRGIVVD YLNEIAKYTG WEYEYIDTDG
     ETMVDEFLEG RYDLMGGTYY QEGLEEYFAY PDYNTGYSKS VLLASREDDS IKAYDWKSLS
     GKTIGVYERA VENIRRLKVF LDSNGIDCTL KTYSAEQLTD GNMYSYLENG EVDMILGNLG
     SDADVFRVVA EFDSQPHYIV TKPEDKEILD GLNMALGKIV DSNPHFAQER YDANIQDSST
     ANITLNDEEK KYVEEKKTVS VAVLKEWHPL YCRELKKDLH DGIIPDILEE IKEFSGLTFS
     YKYVDSYAEG LQMVENGEAD LFGAFLGTDE EAAQKEMALT KPYVVLNDII ERNKSVSYPS
     EGLTGAVLEG RELPAEIEAS EVKYYSNTAE ALRAVDQGEA DFYYGVSAIM EQEIQNHHFT
     NVVPNTLIND RNDISFAMKR PAPGQLLTIM NKAINSLSST QKDTIANQNM ISSGTGEMTI
     IEMIYANPLM FVVICGVVFL LIVILILVMA RYRIHAVRMQ NSLAKAEKEN RAKGEFLSRM
     SHEIRTPMNA IVGLSDLTCM MDDVPETVRV NLSKIRSSSR YLLGLISDIL DMSRIEQDMM
     TIVREPFSIG QVMNELESMM TAEAGRRELE FKLDLRIKSD RLIGDAVRLK QVLMNLISNA
     FKFTSAGGRI RVDVTETEAS AEEAVFCFRV ADNGIGISEK DQERIFESFE QVGTNYSKSQ
     GTGLGLAISK NIVELMGGKL ELKSEIGKGS EFYFTAAFPT AASEEVHDES PAVDMPKRYL
     RDMCILLAED NDLNAEIAEE LLEMQGAAVR RARNGRDAVK MFEDSAPGEF HAILMDIQMP
     VMDGLEACRV IRGMKREDAA VIPVIAMTAN TFKEDVDMAA EAGMDGFVTK PVDVEYLYQV
     LCKAVRRDRP AQPDVL
//
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