RCSC_SALTI
ID RCSC_SALTI Reviewed; 948 AA.
AC Q56128;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 25-MAY-2022, entry version 162.
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};
GN OrderedLocusNames=STY2496, t0594;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 846-948.
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=8626298; DOI=10.1128/jb.178.6.1691-1698.1996;
RA Virlogeux I., Waxin H., Ecobichon C., Lee J.O., Popoff M.Y.;
RT "Characterization of the rcsA and rcsB genes from Salmonella typhi: rcsB
RT through tviA is involved in regulation of Vi antigen synthesis.";
RL J. Bacteriol. 178:1691-1698(1996).
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; AL513382; CAD07502.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68299.1; -; Genomic_DNA.
DR EMBL; X87830; CAA61095.1; -; Genomic_DNA.
DR RefSeq; NP_456815.1; NC_003198.1.
DR RefSeq; WP_000876074.1; NZ_WSUR01000051.1.
DR AlphaFoldDB; Q56128; -.
DR SMR; Q56128; -.
DR STRING; 220341.16503497; -.
DR EnsemblBacteria; AAO68299; AAO68299; t0594.
DR KEGG; stt:t0594; -.
DR KEGG; sty:STY2496; -.
DR PATRIC; fig|220341.7.peg.2528; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_15_6_6; -.
DR OMA; TRCWLAV; -.
DR BRENDA; 2.7.13.3; 5557.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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:0046777; P:protein autophosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.10970; -; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 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; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..948
FT /note="Sensor histidine kinase RcsC"
FT /id="PRO_0000074857"
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; 106237 MW; AE3A21701265A865 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 PKGVDRLVTA 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 ALKQTLAVYA ERVRKTRA
