RCSC_ECOLI
ID RCSC_ECOLI Reviewed; 949 AA.
AC P0DMC5; P14376; P76457; P97170; P97202; Q47586;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 56.
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};
DE AltName: Full=Capsular synthesis regulator component C;
GN Name=rcsC {ECO:0000255|HAMAP-Rule:MF_00979};
GN OrderedLocusNames=b2218, JW5917/JW5920;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12;
RX PubMed=2404948; DOI=10.1128/jb.172.2.659-669.1990;
RA Stout V., Gottesman S.;
RT "RcsB and RcsC: a two-component regulator of capsule synthesis in
RT Escherichia coli.";
RL J. Bacteriol. 172:659-669(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=10564486; DOI=10.1046/j.1365-2958.1999.01605.x;
RA Carballes F., Bertrand C., Bouche J.P., Cam K.;
RT "Regulation of Escherichia coli cell division genes ftsA and ftsZ by the
RT two-component system rcsC-rcsB.";
RL Mol. Microbiol. 34:442-450(1999).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND PHOSPHORELAY.
RX PubMed=11758943; DOI=10.1271/bbb.65.2364;
RA Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
RT "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway
RT involved in capsular synthesis in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
RN [7]
RP FUNCTION, AUTOPHOSPHORYLATION, AND PHOSPHORELAY.
RC STRAIN=K12;
RX PubMed=11309126; DOI=10.1046/j.1365-2958.2001.02393.x;
RA Takeda S.-H., Fujisawa Y., Matsubara M., Aiba H., Mizuno T.;
RT "A novel feature of the multistep phosphorelay in Escherichia coli: a
RT revised model of the RcsC->YojN->RcsB signalling pathway implicated in
RT capsular synthesis and swarming behaviour.";
RL Mol. Microbiol. 40:440-450(2001).
RN [8]
RP FUNCTION AS A KINASE AND A PHOSPHATASE, AND MUTAGENESIS OF HIS-479 AND
RP ASP-875.
RX PubMed=11807084; DOI=10.1128/jb.184.4.1204-1208.2002;
RA Clarke D.J., Joyce S.A., Toutain C.M., Jacq A., Holland I.B.;
RT "Genetic analysis of the RcsC sensor kinase from Escherichia coli K-12.";
RL J. Bacteriol. 184:1204-1208(2002).
RN [9]
RP FUNCTION.
RC STRAIN=K12 / ST001;
RX PubMed=13129944; DOI=10.1128/jb.185.19.5735-5746.2003;
RA Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
RA Mizuno T.;
RT "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB
RT phosphorelay system in Escherichia coli.";
RL J. Bacteriol. 185:5735-5746(2003).
RN [10]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=14651646; DOI=10.1046/j.1365-2958.2003.03815.x;
RA Ferrieres L., Clarke D.J.;
RT "The RcsC sensor kinase is required for normal biofilm formation in
RT Escherichia coli K-12 and controls the expression of a regulon in response
RT to growth on a solid surface.";
RL Mol. Microbiol. 50:1665-1682(2003).
RN [11]
RP INTERACTION WITH RCSD.
RX PubMed=15476819; DOI=10.1016/j.jmb.2004.08.096;
RA Rogov V.V., Bernhard F., Loehr F., Doetsch V.;
RT "Solution structure of the Escherichia coli YojN histidine-
RT phosphotransferase domain and its interaction with cognate phosphoryl
RT receiver domains.";
RL J. Mol. Biol. 343:1035-1048(2004).
RN [12]
RP ACTIVITY REGULATION, AND PHOSPHORELAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16166540; DOI=10.1128/jb.187.19.6770-6778.2005;
RA Majdalani N., Heck M., Stout V., Gottesman S.;
RT "Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia
RT coli.";
RL J. Bacteriol. 187:6770-6778(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [14]
RP ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100;
RX PubMed=19240136; DOI=10.1101/gad.499409;
RA Tschowri N., Busse S., Hengge R.;
RT "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light
RT response of Escherichia coli.";
RL Genes Dev. 23:522-534(2009).
RN [15]
RP STRUCTURE BY NMR OF 700-949, AND INTERACTION WITH RCSD.
RX PubMed=17005198; DOI=10.1016/j.jmb.2006.07.052;
RA Rogov V.V., Rogova N.Y., Bernhard F., Koglin A., Lohr F., Dotsch V.;
RT "A new structural domain in the Escherichia coli RcsC hybrid sensor kinase
RT connects histidine kinase and phosphoreceiver domains.";
RL J. Mol. Biol. 364:68-79(2006).
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. RcsC has also phosphatase activity. The system
CC controls expression of genes involved in colanic acid capsule
CC synthesis, biofilm formation and cell division. {ECO:0000255|HAMAP-
CC Rule:MF_00979, ECO:0000269|PubMed:10564486,
CC ECO:0000269|PubMed:11309126, ECO:0000269|PubMed:11758943,
CC ECO:0000269|PubMed:11807084, ECO:0000269|PubMed:13129944,
CC ECO:0000269|PubMed:14651646}.
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 -!- ACTIVITY REGULATION: The Rcs phosphorelay may be activated by RcsF.
CC DjlA, LolA and OmpG might act as a regulator of the phosphorelay.
CC Activity is probably up-regulated by YmgA/AriR, and possibly down-
CC regulated by YcgZ, all 3 are connector proteins providing additional
CC signal input into signaling system. {ECO:0000269|PubMed:11758943,
CC ECO:0000269|PubMed:16166540, ECO:0000269|PubMed:19240136}.
CC -!- SUBUNIT: Interacts with RcsD. {ECO:0000255|HAMAP-Rule:MF_00979,
CC ECO:0000269|PubMed:15476819, ECO:0000269|PubMed:17005198}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00979, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2404948}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00979, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2404948}.
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.
CC -!- MISCELLANEOUS: There is a close linkage between the Rcs and PhoQ/P
CC signaling systems, and both signaling systems respond to certain
CC external divalent cations (zinc and magnesium).
CC {ECO:0000305|PubMed:13129944}.
CC -!- SIMILARITY: Belongs to the RcsC family. {ECO:0000255|HAMAP-
CC Rule:MF_00979}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA16001.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA16014.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA16014.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M28242; AAA24503.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75278.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16001.2; ALT_FRAME; Genomic_DNA.
DR EMBL; AP009048; BAA16014.1; ALT_SEQ; Genomic_DNA.
DR PIR; H64991; BVECCC.
DR RefSeq; NP_416722.2; NC_000913.3.
DR RefSeq; WP_000876011.1; NZ_SSZK01000030.1.
DR PDB; 2AYX; NMR; -; A=700-949.
DR PDB; 2AYY; NMR; -; A=700-816.
DR PDB; 2AYZ; NMR; -; A=817-949.
DR PDBsum; 2AYX; -.
DR PDBsum; 2AYY; -.
DR PDBsum; 2AYZ; -.
DR AlphaFoldDB; P0DMC5; -.
DR BMRB; P0DMC5; -.
DR SMR; P0DMC5; -.
DR IntAct; P0DMC5; 1.
DR STRING; 511145.b2218; -.
DR iPTMnet; P0DMC5; -.
DR jPOST; P0DMC5; -.
DR PaxDb; P0DMC5; -.
DR PRIDE; P0DMC5; -.
DR EnsemblBacteria; AAC75278; AAC75278; b2218.
DR EnsemblBacteria; BAA16001; BAA16001; BAA16001.
DR EnsemblBacteria; BAA16014; BAA16014; BAA16014.
DR GeneID; 948993; -.
DR KEGG; ecj:JW5917; -.
DR KEGG; ecj:JW5920; -.
DR KEGG; eco:b2218; -.
DR PATRIC; fig|511145.12.peg.2307; -.
DR EchoBASE; EB0815; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_69_12_6; -.
DR OMA; TRCWLAV; -.
DR PhylomeDB; P0DMC5; -.
DR BioCyc; EcoCyc:RCSC-MON; -.
DR BioCyc; MetaCyc:RCSC-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P0DMC5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISM:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:EcoCyc.
DR GO; GO:0018217; P:peptidyl-aspartic acid phosphorylation; ISM:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; ISM:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
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 3D-structure; ATP-binding; Capsule biogenesis/degradation;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..949
FT /note="Sensor histidine kinase RcsC"
FT /id="PRO_0000074856"
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:0000305"
FT MOD_RES 875
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MUTAGEN 479
FT /note="H->Q: Does not induce cps operon expression. Retains
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11807084"
FT MUTAGEN 875
FT /note="D->Q: Does not induce cps operon expression. Lack of
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11807084"
FT CONFLICT 129..130
FT /note="MR -> IG (in Ref. 1; AAA24503)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="T -> S (in Ref. 1; AAA24503)"
FT /evidence="ECO:0000305"
FT TURN 703..706
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 707..712
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 716..726
FT /evidence="ECO:0007829|PDB:2AYX"
FT TURN 727..730
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 731..735
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 746..752
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 759..765
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:2AYY"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 790..799
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 826..833
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 834..847
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 849..854
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 858..866
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 870..878
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 884..894
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 899..908
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 909..916
FT /evidence="ECO:0007829|PDB:2AYX"
FT STRAND 920..926
FT /evidence="ECO:0007829|PDB:2AYX"
FT HELIX 929..947
FT /evidence="ECO:0007829|PDB:2AYX"
SQ SEQUENCE 949 AA; 106506 MW; E37E9D70EC944A78 CRC64;
MKYLASFRTT LKASRYMFRA LALVLWLLIA FSSVFYIVNA LHQRESEIRQ EFNLSSDQAQ
RFIQRTSDVM KELKYIAENR LSAENGVLSP RGRETQADVP AFEPLFADSD CSAMSNTWRG
SLESLAWFMR YWRDNFSAAY DLNRVFLIGS DNLCMANFGL RDMPVERDTA LKALHERINK
YRNAPQDDSG SNLYWISEGP RPGVGYFYAL TPVYLANRLQ ALLGVEQTIR MENFFLPGTL
PMGVTILDEN GHTLISLTGP ESKIKGDPRW MQERSWFGYT EGFRELVLKK NLPPSSLSIV
YSVPVDKVLE RIRMLILNAI 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 GIPLEKAPGE
WVHSVAAPHE LPALLARIYL IEMESDDPAN ALPSTDKAVS DNDDMMILVV DDHPINRRLL
ADQLGSLGYQ CKTANDGVDA LNVLSKNHID IVLSDVNMPN MDGYRLTQRI RQLGLTLPVI
GVTANALAEE KQRCLESGMD SCLSKPVTLD VIKQTLTLYA ERVRKSRDS
