RPRX_BACFR
ID RPRX_BACFR Reviewed; 519 AA.
AC Q08408; Q64PH4;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Sensor protein RprX;
DE EC=2.7.13.3;
GN Name=rprX; OrderedLocusNames=BF3865;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8469117; DOI=10.1111/j.1365-2958.1993.tb01167.x;
RA Rasmussen B.A., Kovacs E.;
RT "Cloning and identification of a two-component signal-transducing
RT regulatory system from Bacteroides fragilis.";
RL Mol. Microbiol. 7:765-776(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC -!- FUNCTION: Member of the two-component regulatory system RprX/RprY. May
CC activate RprY by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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DR EMBL; S59000; AAB26173.2; -; Genomic_DNA.
DR EMBL; AP006841; BAD50607.1; -; Genomic_DNA.
DR PIR; S33661; S33661.
DR RefSeq; WP_005790953.1; NZ_UYXF01000018.1.
DR RefSeq; YP_101141.1; NC_006347.1.
DR AlphaFoldDB; Q08408; -.
DR SMR; Q08408; -.
DR STRING; 295405.BF3865; -.
DR EnsemblBacteria; BAD50607; BAD50607; BF3865.
DR GeneID; 66331525; -.
DR KEGG; bfr:BF3865; -.
DR PATRIC; fig|295405.11.peg.3710; -.
DR HOGENOM; CLU_026375_1_0_10; -.
DR OMA; KFYREHT; -.
DR BRENDA; 2.7.13.3; 755.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; NAS:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; NAS:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..519
FT /note="Sensor protein RprX"
FT /id="PRO_0000074864"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 296..517
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 299
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 20
FT /note="L -> W (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="K -> R (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="L -> S (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> I (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="D -> E (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> N (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="I -> F (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> F (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="T -> S (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="I -> M (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="N -> D (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="V -> C (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="N -> I (in Ref. 1; AAB26173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 59977 MW; 88937AC6695218C7 CRC64;
MKKSTIWILG IIMGLSFLSL LYLQVSYIEE MVKMRKEQFN TSVRNALFQV SKDVEYDETQ
RWLLEDITEA ERRALAQSSS TTEQKNGLIQ QSERYRFKSP DGTLYSEFEL KMITTEPSKV
PKAMISERHG RNTIPQTSRS LTDAIKNRYM YQRFLLDDVA LRMIYKASDK SIGERVNFKK
LDNYLKSNFI NNGVELLYHF SVIDKDGREV YRCSDYEDGG SEDSYTQPLF QNDPPAKMSI
VKVHFPGKKD YIFDSVSFMI PSMIFTIVLL ITFIFTIYIV FRQKKLTEMK NDFINNMTHE
FKTPISTISL AAQMLKDPAV GKSPQMFQHI SGVINDETKR LRFQVEKVLQ MSMFDRQKAT
LKMKELDANE LITGVINTFA LKVERYNGKI TSNLEATNPV IFADEMHITN VIFNLMDNAV
KYKKPEEDLV LNVRTWNEPG KLMISIQDNG IGIKKENLKK VFDKFYRVHT GNLHDVKGFG
LGLAYVKKII QDHKGTIRAE SELNVGTKFI IALPLLKND
