ID B7N5I0_ECOLU Unreviewed; 933 AA.
AC B7N5I0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Sensor histidine kinase RcsC {ECO:0000256|HAMAP-Rule:MF_00979};
DE EC=2.7.13.3 {ECO:0000256|HAMAP-Rule:MF_00979};
GN Name=rcsC {ECO:0000256|HAMAP-Rule:MF_00979,
GN ECO:0000313|EMBL:CAR13739.1};
GN OrderedLocusNames=ECUMN_2555 {ECO:0000313|EMBL:CAR13739.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR13739.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsC functions as a membrane-
CC associated protein kinase that phosphorylates RcsD in response to
CC environmental signals. The phosphoryl group is then transferred to the
CC response regulator RcsB. {ECO:0000256|HAMAP-Rule:MF_00979}.
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 ECO:0000256|HAMAP-Rule:MF_00979};
CC -!- SUBUNIT: Interacts with RcsD. {ECO:0000256|HAMAP-Rule:MF_00979}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00979}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00979}.
CC -!- PTM: Autophosphorylated. Activation probably requires a transfer of a
CC phosphate group from a His in the transmitter domain to an Asp in the
CC receiver domain. {ECO:0000256|HAMAP-Rule:MF_00979}.
CC -!- SIMILARITY: Belongs to the RcsC family. {ECO:0000256|HAMAP-
CC Rule:MF_00979}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00979}.
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DR EMBL; CU928163; CAR13739.1; -; Genomic_DNA.
DR RefSeq; YP_002413267.2; NC_011751.1.
DR AlphaFoldDB; B7N5I0; -.
DR STRING; 585056.ECUMN_2555; -.
DR KEGG; eum:ECUMN_2555; -.
DR PATRIC; fig|585056.7.peg.2736; -.
DR HOGENOM; CLU_000445_15_6_6; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.40.50.10970; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00979; RcsC; 1.
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; IPR030856; RcsC.
DR InterPro; IPR038388; RcsC_C_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR019017; Sig_transdc_His_kin_a/b-loop_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF09456; RcsC; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS51426; ABL; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00979};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00979};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00979};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00979}; Transferase {ECO:0000256|HAMAP-Rule:MF_00979};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00979};
KW Two-component regulatory system {ECO:0000256|HAMAP-Rule:MF_00979}.
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979"
FT DOMAIN 460..676
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 689..789
FT /note="ABL"
FT /evidence="ECO:0000259|PROSITE:PS51426"
FT DOMAIN 810..924
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 463
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979"
FT MOD_RES 859
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 933 AA; 104631 MW; 4D91CE9479400D35 CRC64;
MFRALALVLW LLIAFSSVFY IVNALHQRES EIRQEFNLSS DQAQRFIQRT SDVMKELKYI
AENRLSAENG VLSPRGRETQ TDVPAFEPLF ADSDCSAMSN TWRGSLESLA WFMRYWRDNF
SAAYDLNRVF LIGSDNLCMA NFGLRDMPVE RDTALKALHE RINKYRNAPQ DDSGSNLYWI
SEGPRPGVGY FYALTPVYLA NRLQALLGVE QTIRMENFFL PGTLPMGVTI LDENGHTLIS
LTGPESKIKG DPRWMQERSW FGYTEGFREL VLKKNLPPSS LSIVYSVPVD KVLERIRMLI
LNAILLNVLA GAALFTLARM YERRIFIPAE SDALRLEEHE QFNRKIVASA PVGICILRTA
DGVNILSNEL AHTYLNMLTH EDRQRLTQII CGQQVNFVDV LTSNNTNLQI SFVHSRYRNE
NVAICVLVDV SSRVKMEESL QEMAQAAEQA SQSKSMFLAT VSHELRTPLY GIIGNLDLLQ
TKELPKGVDR LVTAMNNSSS LLLKIISDIL DFSKIESEQL KIEPREFSPR EVMNHITANY
LPLVVRKQLG LYCFIEPDVP VALNGDPMRL QQVISNLLSN AIKFTDTGCI VLHVRADGDY
LSIRVRDTGV GIPAKEVVRL FDPFFQVGTG VQRNFQGTGL GLAICEKLIS MMDGDISVDS
EPGMGSQFTV RIPLYGAQYP QKKGVEGLSG KRCWLAVRNA SLCQFLENSL QRSGIVVTTY
EGQEPTPEDV LITDEVVSKK WQGRAVVTFC RRHIGIPLEK APGEWVHSVA APHELPALLA
RIYLIEMESD DPANALPSTD KAVSDNDDMM ILVVDDHPIN RRLLADQLGS LGYQCKTAND
GVDALNVLSK NHIDIVLSDV NMPNMDGYRL TQRIRQLGLT LPVIGVTANA LAEEKQRCLE
SGMDSCLSKP VTLDVIKQTL TVYAERVRKS RES
//
