CSEC_STRCO
ID CSEC_STRCO Reviewed; 507 AA.
AC Q9ZEP3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Sensor protein CseC;
DE EC=2.7.13.3;
GN Name=cseC; OrderedLocusNames=SCO3359; ORFNames=SCE94.10;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN TRANSCRIPTIONAL
RP ACTIVATION OF SIGMA E.
RC STRAIN=A3(2) / M600;
RX PubMed=10411727; DOI=10.1046/j.1365-2958.1999.01452.x;
RA Paget M.S.B., Leibowitz E., Buttner M.J.;
RT "A putative two-component signal transduction system regulates sigE, a
RT sigma factor required for normal cell wall integrity in Streptomyces
RT coelicolor A3(2).";
RL Mol. Microbiol. 33:97-107(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Member of the two-component regulatory system CseB/CseC
CC involved in the stability of the cell envelope, through activation of
CC transcription of RNA polymerase sigma-E factor. CseC functions as a
CC membrane-associated protein kinase that phosphorylates CseB in response
CC to changes in the cell envelope. {ECO:0000269|PubMed:10411727}.
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}.
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DR EMBL; AJ131213; CAA10326.1; -; Genomic_DNA.
DR EMBL; AL939116; CAB40859.1; -; Genomic_DNA.
DR PIR; T36370; T36370.
DR RefSeq; NP_627567.1; NC_003888.3.
DR RefSeq; WP_011028932.1; NZ_VNID01000023.1.
DR AlphaFoldDB; Q9ZEP3; -.
DR SMR; Q9ZEP3; -.
DR STRING; 100226.SCO3359; -.
DR PRIDE; Q9ZEP3; -.
DR GeneID; 1098796; -.
DR KEGG; sco:SCO3359; -.
DR PATRIC; fig|100226.15.peg.3421; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_4_11; -.
DR InParanoid; Q9ZEP3; -.
DR OMA; HNAARVS; -.
DR PhylomeDB; Q9ZEP3; -.
DR Proteomes; UP000001973; 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; IBA:GO_Central.
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 1: Evidence at protein level;
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..507
FT /note="Sensor protein CseC"
FT /id="PRO_0000314483"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 204..260
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 268..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 507 AA; 54266 MW; B59A28BF828207EA CRC64;
MRGFFRQRRS VSPPGHPYDR TGPGEHAGPG ARTGPGGRPR VLGVRGLRAR GIRTGLRWKL
SAAIALVGAL VAIALSLVVH NAARVSMLDN ARDLADDRVL IAQRNYELSG RQNFPNAQID
DPALPPELRR KIDAGRRATY VSERPDGVTD IWAAVPLKDG HVMSLHSGFT DRSADILSDL
DQALVIGSIA VVLGGSALGV LIGGQLSRRL REAAAAANRV ASGEPDVRVR DAIGGVVRDE
TDDVARAVDA MADALQQRIE AERRVTADIA HELRTPVTGL LTAAELLPPG RPTELVLDRA
KAMRTLVEDV LEVARLDGAS ERAELQDIML GDFVSRRVAA KDPAVEVRVI HESEVTTDPR
RLERVLFNLL ANAARHGRSP VEVSVEGRVI RVRDHGPGFP EDLLAEGPSR FRTGSTDRAG
RGHGLGLTIA AGQARVLGAR LTFRNVRPAG APAHIPAEGA VAVLWLPEHA PTNTGSYPML
PDRSKSGASS SARDMSREAS QGMSRKP
