ID Q8XE40_ECO57 Unreviewed; 890 AA.
AC Q8XE40; A0A0H3JFQ5; A0A6M0JLQ7; Q7AC52;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Phosphotransferase RcsD {ECO:0000256|HAMAP-Rule:MF_00980};
DE EC=2.7.2.- {ECO:0000256|HAMAP-Rule:MF_00980};
DE AltName: Full=Phosphotransfer intermediate RcsD {ECO:0000256|HAMAP-Rule:MF_00980};
GN Name=rcsD {ECO:0000256|HAMAP-Rule:MF_00980,
GN ECO:0000313|EMBL:BAB36528.1};
GN ORFNames=ECs_3105 {ECO:0000313|EMBL:BAB36528.1};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB36528.1, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB36528.1, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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.
CC {ECO:0000256|HAMAP-Rule:MF_00980}.
CC -!- SUBUNIT: Interacts with RcsC and RcsB. {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00980}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
CC -!- PTM: Phosphorylated by RcsC. {ECO:0000256|HAMAP-Rule:MF_00980}.
CC -!- SIMILARITY: Belongs to the RcsD family. {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00980}.
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DR EMBL; BA000007; BAB36528.1; -; Genomic_DNA.
DR RefSeq; NP_311132.1; NC_002695.1.
DR RefSeq; WP_001249123.1; NZ_VOAI01000001.1.
DR AlphaFoldDB; Q8XE40; -.
DR STRING; 155864.Z3475; -.
DR GeneID; 916813; -.
DR KEGG; ecs:ECs_3105; -.
DR PATRIC; fig|386585.9.peg.3239; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_009611_0_0_6; -.
DR OMA; TWRYATW; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IEA:InterPro.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.50.11620; Phosphotransferase RcsD, RcsD-ABL domain; 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 PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00980};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00980};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00980};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00980}; Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00980};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00980};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|HAMAP-Rule:MF_00980}.
FT TRANSMEM 22..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00980"
FT MOD_RES 842
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00980"
SQ SEQUENCE 890 AA; 100361 MW; E7BDF9D66771A350 CRC64;
MRQKETTATT RFSLLPGSIT RFFLLLIIVL LVTMGVMVQS AVNAWLKDKS YQIVDITHAI
QKRVDTWRYV 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 RHFSSRSTES LPNTAVNNEL RILRAINEEI
VSLLPLGLLV HDQESNRTVI SNKIADHLLP HLNLQNITTM AEQHQGIIQA TINNELYEIR
MFRSQVAPRT QIFIIRDQDR EVLVNKKLKQ AQRLYEKNQQ GRMTFMKNIG 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
//
