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Database: UniProt
Entry: A0A2U2PBX7_9SPHI
LinkDB: A0A2U2PBX7_9SPHI
Original site: A0A2U2PBX7_9SPHI 
ID   A0A2U2PBX7_9SPHI        Unreviewed;       646 AA.
AC   A0A2U2PBX7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DDR33_19835 {ECO:0000313|EMBL:PWG78907.1};
OS   Pararcticibacter amylolyticus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pararcticibacter.
OX   NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG78907.1, ECO:0000313|Proteomes:UP000245647};
RN   [1] {ECO:0000313|EMBL:PWG78907.1, ECO:0000313|Proteomes:UP000245647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG78907.1,
RC   ECO:0000313|Proteomes:UP000245647};
RA   Cai Y.;
RT   "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PWG78907.1}.
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DR   EMBL; QEAS01000019; PWG78907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2PBX7; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000245647; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 2.
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; 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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 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; 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; 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; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245647}.
FT   DOMAIN          1..73
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          78..131
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          280..500
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          524..642
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         573
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   646 AA;  73844 MW;  71C93AC76AA93AEE CRC64;
     MDLLYKTIVE DSLAGYFDWD LRSNVIYMTP AFKAMMGYQD YEVENSLDAW KNLIHPDDKE
     GVNLAFKEHV QSRGEIKFTV EGRYRHKNGS YIYLLTLGKV VEWGIEGEPL RAVGCHVDIT
     KQKAAEAKSY EAELSIRHSR EQLRNFIRYC PVAVAMLDHN MNYIEASNLW ISLYGAPDRD
     VSGKNHYELF SWIPQRWKDA HRRGLSGEVV KCDEDEFMGS GKREWIRYEI RPWYNESGQI
     GGIIIFTEII TDYVKTREAL IRAREEAENA ARMESLFLST MSHEIRTPLN AVIGFTHLLL
     KDPRPDQTES LNILKFSAEH LLVLINDILD FNKIEAGKLE FENVDFSIAG LISNIKAAFQ
     EKAAEKAIGL KLLLDDDLPP MVKGDPVRLG QVLNNLISNA VKFTNQGKVT IAAHLISRNT
     TDTVVEIEIR DTGIGIRPDK QEKIFESFSQ ASVDITRNYG GTGLGLAITK RLLQLMGSQI
     YLESEEGKGA RFYFTLRLDS SDKHPFDEKI LTEQVEFKSF KGVKVLIAED NKINVLVARQ
     FLKHWDVECD VVENGLQALN MVQQHHYSVI LMDLQMPVMD GYEATKKIRE LTDEKYQKLP
     IIALTASVMV DHRDKAFFVG FNDYVGKPFT PRELYSKISK YVNPVD
//
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