ID   RCSC_ECOLX              Reviewed;         949 AA.
AC   P0DMC6; P14376; P76457; P97170; P97202; Q47586;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
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};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN CAPSULAR POLYSACCHARIDE
RP   SYNTHESIS.
RC   STRAIN=O9:K30:H12;
RX   PubMed=8366025; DOI=10.1128/jb.175.17.5384-5394.1993;
RA   Jayaratne P., Keenleyside W.J., Maclachlan P.R., Dodgson C., Whitfield C.;
RT   "Characterization of rcsB and rcsC from Escherichia coli O9:K30:H12 and
RT   examination of the role of the rcs regulatory system in expression of group
RT   I capsular polysaccharides.";
RL   J. Bacteriol. 175:5384-5394(1993).
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 (By similarity). Involved in regulation of K30
CC       capsular polysaccharide synthesis. {ECO:0000255|HAMAP-Rule:MF_00979,
CC       ECO:0000269|PubMed:8366025}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24505.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L11272; AAA24505.1; ALT_INIT; Genomic_DNA.
DR   PIR; H64991; BVECCC.
DR   AlphaFoldDB; P0DMC6; -.
DR   BMRB; P0DMC6; -.
DR   SMR; P0DMC6; -.
DR   STRING; 585034.ECIAI1_2302; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   BRENDA; 2.7.13.3; 2026.
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   1: Evidence at protein level;
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..949
FT                   /note="Sensor histidine kinase RcsC"
FT                   /id="PRO_0000425316"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..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..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00979"
FT   TOPO_DOM        336..949
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   949 AA;  106364 MW;  556D7C967969CD69 CRC64;
     MKYLASFRTT LKASRYMFRA LALVLWLLIA FSSVFYIVNA LHQRESEIRQ EFNLSSDQAQ
     RFIQRTSDVM KELKYIAENR LSAENGVLSP RGRETQADVP AFEPLFADSD CSAMSNTWRG
     SLESLAWFIG YWRDNFSAAY DLNRVFLIGS DNLCMANFGL RDMPVERDTA LKALHERINK
     YRNAPQDDSG SNLYWISEGP RPGVGYFYAL TPVYLANRLQ ALLGVEQTIR MENFFLPGTL
     PMGVTILDEN GHTLISLTGP ESKIKGDPRW MQERSWFGYT EGFRELVLKK NLPPSSLSIV
     YSVPVDKVLE RIRMVILNAI LLNVLAGAAL FTLARMYERR IFIPAESDAL RLEEHEQFNR
     KIVASAPVGI CILRTADGVN ILSNELAHTY LNMLTHEDRQ RLTQIICGQQ VNFVDVLTSN
     NTNLQISFVH SRYRNENVAI CVLVDVSSRV KMEESLQEMA QAAEQASQSK SMFLATVSHE
     LRTPLYGIIG NLDLLQTKEL PKGVDRLVTA MNNSSSLLLK IISDILDFSK IESEQLKIEP
     REFSPREVMN HITANYLPLV VRKQLGLYCF IEPDVPVALN GDPMRLQQVI SNLLSNAIKF
     TDTGCIVLHV RADGDYLSIR VRDTGVGIPA KEVVRLFDPF FQVGTGVQRN FQGTGLGLAI
     CEKLISMMDG DISVDSEPGM GSQFTVRIPL YGAQYPQKKG VEGLSGKRCW LAVRNASLCQ
     FLETSLQRSG IVVTTYEGQE PTPEDVLITD EVVSKKWQGR AVVTFCRRHI GIPLEEAPGE
     WVHSVAAPHE LPALLARIYL IEMESDDPAN ALPSTDKAVS DNDDMMILVV DDHPINRRLL
     ADQLGSLGYQ CKTANDGVDA LNVLSKNHID IVLSDVNMPN MDGYRLTQRT RQLGLTLPVI
     GVTANALAEE KQRCLESGMD SCLSKPVTLD VIKQTLTVYA ERVRKSRES