ID   CSEC_STRAW              Reviewed;         487 AA.
AC   Q82EB2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Sensor protein CseC;
DE            EC=2.7.13.3;
GN   Name=cseC; OrderedLocusNames=SAV_4703;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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; BA000030; BAC72415.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q82EB2; -.
DR   SMR; Q82EB2; -.
DR   STRING; 227882.SAV_4703; -.
DR   PRIDE; Q82EB2; -.
DR   EnsemblBacteria; BAC72415; BAC72415; SAVERM_4703.
DR   KEGG; sma:SAVERM_4703; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_4_11; -.
DR   OMA; HNAARVS; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
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   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..487
FT                   /note="Sensor protein CseC"
FT                   /id="PRO_0000314482"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..262
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          270..472
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         273
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   487 AA;  51616 MW;  B5B108F884C3A5EE CRC64;
     MRGNLRRPGP AGTAGPGRTG IRTSADGGRA RPRTGAGTGV RAGVRSGVVG VGAGIRTGVR
     WKISAAIALV GALVALALSL VVHNAARVSM LDNARDLADE RIQVAERMYE AGRAQSFGVK
     LDDPAIPRDL MMKVTQGRRA TYVADGPHGV PDIWAAVPLK DGRVLSLHTR FTDRSADIMK
     DLDQALIIGS IAVVFGGSAL GVLIGGQLSR RLRKAAAAAN QVAQGERDVR VRDAIGGVVR
     DETDDLARAV DAMADALQQR IEAERRVTAD IAHELRTPVT GLLTAAELLP PGRPTELVRD
     RAQAMRTLVE DVLEVARLDG ASERAELQDI MLGEFVSRRV AAKDADIEVR VVHESEVTTD
     PRRLERVLFN LLANAARHGK PPIEVSVEGR VIRVRDHGPG FPEELLADGP RRFRTGSTDR
     AGHGHGLGLT IAAGQARVLG ARLTFRNVRP AGAPGDVPAE GAVAVLWLPE HAPTNTGSFP
     MLPLSGG