GenomeNet

Database: UniProt
Entry: B9XQ60_PEDPL
LinkDB: B9XQ60_PEDPL
Original site: B9XQ60_PEDPL 
ID   B9XQ60_PEDPL            Unreviewed;       893 AA.
AC   B9XQ60;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Cflav_PD1201 {ECO:0000313|EMBL:EEF58064.1};
OS   Pedosphaera parvula (strain Ellin514).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF58064.1, ECO:0000313|Proteomes:UP000003688};
RN   [1] {ECO:0000313|EMBL:EEF58064.1, ECO:0000313|Proteomes:UP000003688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin514 {ECO:0000313|EMBL:EEF58064.1,
RC   ECO:0000313|Proteomes:UP000003688};
RX   PubMed=21460084; DOI=10.1128/JB.00299-11;
RA   Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA   Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA   Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT   "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT   Verrucomicrobial isolate from pasture soil.";
RL   J. Bacteriol. 193:2900-2901(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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEF58064.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABOX02000051; EEF58064.1; -; Genomic_DNA.
DR   RefSeq; WP_007417946.1; NZ_ABOX02000051.1.
DR   AlphaFoldDB; B9XQ60; -.
DR   STRING; 320771.Cflav_PD1201; -.
DR   OrthoDB; 5429506at2; -.
DR   Proteomes; UP000003688; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 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; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013656; PAS_4.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
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; SSF55781; GAF domain-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; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF58064.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          102..156
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          155..211
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          404..466
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          468..520
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          533..755
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          778..890
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          377..411
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         829
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   893 AA;  98867 MW;  177F095283AFBFF0 CRC64;
     MKKIEISAPL RISGFYLMLG LGWIFFSNRL LNLLVRDPEL LEKLEIAKGW AFMAVTAGFL
     YFLIQRELAR RQGFQAVLQE SQRTLASLMS SLPGMAYRCM NDQDWTLIFV SQGCVELTGY
     EPDDLLGNKA AAYGALIHEE DREHVWLGVQ KAVQEKREFR LTYRIRTAKG VEKWVWEQGQ
     GVFSSEGEML FLEGLIIDVT ERQQAQQALK LSNERLGLIA RVTGAVVGAT PLAVQAEELA
     DQVRKAFAVD GCVIRVLEEE HMVLLASAGI PKEKLPQQIA LGLGISGEIV NQKRPAAIED
     VHTNPVTAQL FESEPNAYRF KSFAGAPLLV EEKVVGILGI YSEKEVRRFT SADVEHLQIV
     ANHIALAVTN DRLYKAVRTQ NTQLAEQIKE REKAEQLVRE HAALLDKARD AILVCDWENK
     VVFWNESATR LYGWTTSEVI GQSVKELLLR DVAKFETAKS AALENGEWAG ELSQITKEGR
     EILVESRWTL VRDNSGAPRT VFVINTDITE RKKLEVQFLR AQRMESIGTL AGGIAHDLNN
     VLAPILMSIA LLKKMHPEPE TTEVLETLEG SANRGADMIK QVLSYARGVQ GDRITISVAR
     LLEEMEKIMG ETFPKSIRIQ KRMEPSVACL VGDPTQLHQI LLNLCVNARD AMPDGGTLVL
     SAESVLLDDK YKAVSPHAKP GSYVALRVTD TGTGIAPEVK ARIFEPFFTT KEIGKGSGLG
     LSTMLAIVKS HGGFVDVSSE LEKGSTFTVY LPSQTSLDSV SAADTQETAN FVKGNGELVM
     LVEDEAAVRK ATQKALQSFG YQVITANDGA EALAIYRQRQ SEIAVVLTDM MMPIMDGMVM
     IERLRKMHPE VKIVAASGNF SKNWEATGVK AVLAKPYKAE TLLRTLRQVL GNK
//
DBGET integrated database retrieval system