RCSD_ECOLI
ID RCSD_ECOLI Reviewed; 890 AA.
AC P39838; P47725; P47726; P76456;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phosphotransferase RcsD {ECO:0000255|HAMAP-Rule:MF_00980};
DE EC=2.7.2.- {ECO:0000255|HAMAP-Rule:MF_00980};
DE AltName: Full=Phosphotransfer intermediate RcsD {ECO:0000255|HAMAP-Rule:MF_00980};
GN Name=rcsD {ECO:0000255|HAMAP-Rule:MF_00980}; Synonyms=yojN, yojP, yojQ;
GN OrderedLocusNames=b2216, JW2204;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-596.
RC STRAIN=K12 / EMG2;
RA Robison K., Estep P.E., O'Keeffe T., Church G.M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 593-890.
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 [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
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 [8]
RP FUNCTION, 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 [9]
RP FUNCTION, PHOSPHORYLATION AT HIS-842, PHOSPHORELAY, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF HIS-842.
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 [10]
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 [11]
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 [12]
RP STRUCTURE BY NMR OF 775-890, AND INTERACTION WITH RCSC AND RCSB.
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).
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsD is a phosphotransfer intermediate
CC between the sensor kinase RcsC and the response regulator RcsB. It
CC acquires a phosphoryl group from RcsC and transfers it to RcsB. The
CC system controls expression of genes involved in colanic acid capsule
CC synthesis, biofilm formation and cell division. {ECO:0000255|HAMAP-
CC Rule:MF_00980, ECO:0000269|PubMed:10564486,
CC ECO:0000269|PubMed:11309126, ECO:0000269|PubMed:11758943,
CC ECO:0000269|PubMed:13129944, ECO:0000269|PubMed:14651646}.
CC -!- SUBUNIT: Interacts with RcsC and RcsB. Has a higher affinity for RcsB
CC than for RcsC. {ECO:0000255|HAMAP-Rule:MF_00980,
CC ECO:0000269|PubMed:15476819}.
CC -!- INTERACTION:
CC P39838; P0DMC7: rcsB; NbExp=5; IntAct=EBI-556803, EBI-369670;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:11309126}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:11309126}.
CC -!- PTM: Phosphorylated by RcsC. {ECO:0000305|PubMed:11309126}.
CC -!- SIMILARITY: Belongs to the RcsD family. {ECO:0000255|HAMAP-
CC Rule:MF_00980}.
CC -!- CAUTION: Contains a histidine kinase domain, but it seems to be non-
CC functional as the highly conserved histidine residue is missing.
CC {ECO:0000305|PubMed:11309126}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81025.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA81026.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA81027.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M28242; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75276.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15999.1; -; Genomic_DNA.
DR EMBL; U38659; AAA81025.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U38659; AAA81026.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U38659; AAA81027.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M28242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F64991; F64991.
DR RefSeq; NP_416720.1; NC_000913.3.
DR RefSeq; WP_001249081.1; NZ_LN832404.1.
DR PDB; 1SR2; NMR; -; A=775-890.
DR PDB; 2KX7; NMR; -; A=688-795.
DR PDBsum; 1SR2; -.
DR PDBsum; 2KX7; -.
DR AlphaFoldDB; P39838; -.
DR BMRB; P39838; -.
DR SMR; P39838; -.
DR BioGRID; 4261921; 3.
DR BioGRID; 851058; 1.
DR DIP; DIP-12815N; -.
DR IntAct; P39838; 4.
DR STRING; 511145.b2216; -.
DR iPTMnet; P39838; -.
DR jPOST; P39838; -.
DR PaxDb; P39838; -.
DR PRIDE; P39838; -.
DR EnsemblBacteria; AAC75276; AAC75276; b2216.
DR EnsemblBacteria; BAA15999; BAA15999; BAA15999.
DR GeneID; 946717; -.
DR KEGG; ecj:JW2204; -.
DR KEGG; eco:b2216; -.
DR PATRIC; fig|1411691.4.peg.19; -.
DR EchoBASE; EB2286; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_009611_0_0_6; -.
DR OMA; TWRYATW; -.
DR PhylomeDB; P39838; -.
DR BioCyc; EcoCyc:EG12385-MON; -.
DR EvolutionaryTrace; P39838; -.
DR PRO; PR:P39838; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IMP:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.11620; -; 1.
DR HAMAP; MF_00980; RcsD; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR030861; Ptransferase_RcsD.
DR InterPro; IPR032306; RcsD_ABL.
DR InterPro; IPR038616; RcsD_ABL_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF16359; RcsD_ABL; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..890
FT /note="Phosphotransferase RcsD"
FT /id="PRO_0000074916"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00980"
FT TOPO_DOM 43..308
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00980"
FT TOPO_DOM 330..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 803..890
FT /note="HPt"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00980"
FT REGION 468..678
FT /note="Histidine-like kinase"
FT MOD_RES 842
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00980,
FT ECO:0000269|PubMed:11309126"
FT MUTAGEN 842
FT /note="H->R: Lack of activity."
FT /evidence="ECO:0000269|PubMed:11309126"
FT CONFLICT 61
FT /note="Q -> L (in Ref. 4; AAA81025)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="K -> E (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="T -> A (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> N (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> G (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> T (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> A (in Ref. 4; AAA81026)"
FT /evidence="ECO:0000305"
FT CONFLICT 598..599
FT /note="ES -> DA (in Ref. 5; M28242)"
FT /evidence="ECO:0000305"
FT STRAND 690..699
FT /evidence="ECO:0007829|PDB:2KX7"
FT HELIX 703..715
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 733..739
FT /evidence="ECO:0007829|PDB:2KX7"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 744..750
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 755..761
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 764..767
FT /evidence="ECO:0007829|PDB:2KX7"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 801..808
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 811..814
FT /evidence="ECO:0007829|PDB:1SR2"
FT TURN 815..817
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 818..831
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 834..851
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 854..868
FT /evidence="ECO:0007829|PDB:1SR2"
FT HELIX 872..889
FT /evidence="ECO:0007829|PDB:1SR2"
SQ SEQUENCE 890 AA; 100372 MW; AE26E2E70E363830 CRC64;
MRQKETTATT RFSLLPGSIT RFFLLLIIVL LVTMGVMVQS AVNAWLKDKS YQIVDITHAI
QKRVDNWRYV TWQIYDNIAA TTSPSSGEGL QETRLKQDVY YLEKPRRKTE ALIFGSHDNS
TLEMTQRMST YLDTLWGAEN VPWSMYYLNG QDNSLVLIST LPLKDLTSGF KESTVSDIVD
SRRAEMLQQA NALDERESFS NMRRLAWQNG HYFTLRTTFN QPGHLATVVA FDLPINDLIP
PGMPLDSFRL EPDATATGNN DNEKEGTDSV SIHFNSTKIE ISSALNSTDM RLVWQVPYGT
LLLDTLQNIL LPLLLNIGLL ALALFGYTTF RHFSSRSTEN VPSTAVNNEL RILRAINEEI
VSLLPLGLLV HDQESNRTVI SNKIADHLLP HLNLQNITTM AEQHQGIIQA TINNELYEIR
MFRSQVAPRT QIFIIRDQDR EVLVNKKLKQ AQRLYEKNQQ GRMIFMKNIG DALKEPAQSL
AESAAKLNAP ESKQLANQAD VLVRLVDEIQ LANMLADDSW KSETVLFSVQ DLIDEVVPSV
LPAIKRKGLQ LLINNHLKAH DMRRGDRDAL RRILLLLMQY AVTSTQLGKI TLEVDQDESS
EDRLTFRILD TGEGVSIHEM DNLHFPFINQ TQNDRYGKAD PLAFWLSDQL ARKLGGHLNI
KTRDGLGTRY SVHIKMLAAD PEVEEEEERL LDDVCVMVDV TSAEIRNIVT RQLENWGATC
ITPDERLISQ DYDIFLTDNP SNLTASGLLL SDDESGVREI GPGQLCVNFN MSNAMQEAVL
QLIEVQLAQE EVTESPLGGD ENAQLHASGY YALFVDTVPD DVKRLYTEAA TSDFAALAQT
AHRLKGVFAM LNLVPGKQLC ETLEHLIREK DVPGIEKYIS DIDSYVKSLL
