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Database: UniProt
Entry: D3RPW4_ALLVD
LinkDB: D3RPW4_ALLVD
Original site: D3RPW4_ALLVD 
ID   D3RPW4_ALLVD            Unreviewed;       721 AA.
AC   D3RPW4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Alvin_2666 {ECO:0000313|EMBL:ADC63575.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC63575.1, ECO:0000313|Proteomes:UP000001441};
RN   [1] {ECO:0000313|EMBL:ADC63575.1, ECO:0000313|Proteomes:UP000001441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC   {ECO:0000313|Proteomes:UP000001441};
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP001896; ADC63575.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3RPW4; -.
DR   STRING; 572477.Alvin_2666; -.
DR   KEGG; alv:Alvin_2666; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_000445_114_15_6; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADC63575.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW   Transferase {ECO:0000313|EMBL:ADC63575.1}.
FT   DOMAIN          98..169
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          173..225
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          222..293
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          361..580
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          604..721
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         653
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   721 AA;  79941 MW;  43CC9F5078F436B6 CRC64;
     MGVLDTALCL NWLQTSTDPK TPLPGLTTSA EFMPLARQVL ASGQPVRQTL ALDEAGCTHR
     LDLILTPMLG PQGETAGAFV GVLDLTETLR VEQALRESET QFRLMFDLAT VGMAVIEPST
     RRVLRVNQRL CRILGYEAGE LLGMSFQDLT HPEDRWHDRR RFRRAVLQLD TDYFTEKRYV
     RKDGTVVWAL VNATFIRDAN GDPVRAVAAI FDITDRREAE TRARDLAAVV ESSSDFIGIA
     GLDRRGLYIN PAGRSLVGLD AEQDITEIRI EDFFMPEDLE QLRQSILPAM ETAGRWAGEF
     RFRHFVTGEP IDVFYDALRI DDPNTGRPLH YATVTRDIRT EKAAEQALRE ADRRKDEFLA
     VLGHELRNPM APIRHAVEIL RALGVDGDPR IRWAIEVLDR QTAHMGRLLD DLLDVSRIVQ
     GRIELEPVEL RVRELVQQAA DGVRALMEEH RHRFVCRLPA PGWRVLGDPV RLSQILLNIL
     VNAANYTPPG GEIRIDSRIE GDSVLIQVRD NGQGMTAEQL DSLFGLFTRG PHAGDADSGG
     LGLGLAIARR LADLHGGCLE ARSEGLGRGT ELCLRLPIFT CARSANLNEP PDCPNVSPAG
     EKPRVLVVDD DPDVVDALAM LLEILGYPVD VARSGPQALE LAQRQCPRVA LLDIGIPGMD
     GLELARRLRT QYPDPKRLKL VALTGLGHEQ ARERSLAAGF DEHLVKPLGR QALLALLESL
     G
//
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