ID RCSC_SALTY Reviewed; 948 AA.
AC P58662;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Sensor histidine kinase RcsC {ECO:0000255|HAMAP-Rule:MF_00979};
DE EC=2.7.13.3 {ECO:0000255|HAMAP-Rule:MF_00979};
GN Name=rcsC {ECO:0000255|HAMAP-Rule:MF_00979}; OrderedLocusNames=STM2271;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000255|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:0000255|HAMAP-Rule:MF_00979};
CC -!- SUBUNIT: Interacts with RcsD. {ECO:0000255|HAMAP-Rule:MF_00979}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00979}; Multi-pass membrane protein {ECO:0000255|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:0000255|HAMAP-Rule:MF_00979}.
CC -!- SIMILARITY: Belongs to the RcsC family. {ECO:0000255|HAMAP-
CC Rule:MF_00979}.
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DR EMBL; AE006468; AAL21172.1; -; Genomic_DNA.
DR RefSeq; NP_461213.1; NC_003197.2.
DR RefSeq; WP_000876078.1; NC_003197.2.
DR AlphaFoldDB; P58662; -.
DR SMR; P58662; -.
DR STRING; 99287.STM2271; -.
DR PaxDb; 99287-STM2271; -.
DR GeneID; 1253793; -.
DR KEGG; stm:STM2271; -.
DR PATRIC; fig|99287.12.peg.2404; -.
DR HOGENOM; CLU_000445_15_6_6; -.
DR OMA; GLRDMPI; -.
DR PhylomeDB; P58662; -.
DR BioCyc; SENT99287:STM2271-MONOMER; -.
DR BRENDA; 2.7.13.3; 5542.
DR PHI-base; PHI:3011; -.
DR Proteomes; UP000001014; 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; 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; 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; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..948
FT /note="Sensor histidine kinase RcsC"
FT /id="PRO_0000074858"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT TOPO_DOM 42..313
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT TOPO_DOM 335..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 357..425
FT /note="PAS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT DOMAIN 476..692
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT DOMAIN 705..805
FT /note="ABL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT DOMAIN 826..940
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 479
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT MOD_RES 875
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
SQ SEQUENCE 948 AA; 106279 MW; BAAD8DA557D5868B CRC64;
MKYLASFRTT LKVSRYLFRA LALLIWLLIA FVSVFYIVNA LHQRESEIRQ EFNLSSDQAQ
RFIQRTSDVM KELKYIAENR LTAENGVMSS RARDDKMVVP DFEPLFADSD CAAMGSAWRG
SLESLAWFMR YWRDNFSAAY DLNRVFLIGS DNLCMANFGL REMPVERDDA LKALHERIMK
YRNAPQEESG NNLFWISQGA RQGVGYFYAL TPVYLANRLQ ALLGVEQSIR MENFFTPGSL
PMGVTIIDEN GHSLISLTGP DGIIKAEPRW MQERSWFGYT PGFRELVLKK SLPPSSLSIV
YSVPVDLVLE RIRILILNAI LLNVLVGAGL FTLARMYERR IFIPAESDAQ RLEEHEQFNR
KIVASAPVGI CILRTIDGVN ILSNELAHTY LNMLTHEDRQ RLTQIICGQQ VNFVDVLTSN
NTNLQISFVH SRYRNENVAI CVLVDVSTRV KMEESLQEMA QAAEQASQSK SMFLATVSHE
LRTPLYGIIG NLDLLQTKEL PKGVERLVTA MNNSSSLLLK IISDILDFSK IESEQLKIEP
REFSPREVMN HITANYLPLV VRKQLGLYCF IEPDVPVSLN GDPMRLQQVI SNLLSNAIKF
TDIGCIVLHV RCDGDYLSIR VRDTGVGIPA KEVVRLFDPF FQVGTGVQRN FQGTGLGLAI
CEKLISMMDG DISVDSEPGM GSQFTLRIPL YGAQYPVKKS VEGLAGTCCW LAVRNTSLCQ
FIETSLARSG VHTQRYEGQE PAADDILIVD DALEHTWQGR AAVVFCRRHI GIPLERAPGE
WVHSVASVHE LPALLARIYS IELDSEALSS ALPTTDKTAD SNDDMMILVV DDHPINRRLL
ADQLGSLGYQ CKTANDGVDA LNVLSKNAID IVLSDVNMPN MDGYRLTQRI RQLGLTLPVV
GVTANALAEE KQRCLESGMD SCLSKPVTLD VLKQTLAVYA ERVRKTRA
//
