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Database: UniProt
Entry: A0A411HHR4_9GAMM
LinkDB: A0A411HHR4_9GAMM
Original site: A0A411HHR4_9GAMM 
ID   A0A411HHR4_9GAMM        Unreviewed;       971 AA.
AC   A0A411HHR4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ELE36_05970 {ECO:0000313|EMBL:QBB69944.1};
OS   Pseudolysobacter antarcticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudolysobacter.
OX   NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB69944.1, ECO:0000313|Proteomes:UP000291562};
RN   [1] {ECO:0000313|EMBL:QBB69944.1, ECO:0000313|Proteomes:UP000291562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB69944.1,
RC   ECO:0000313|Proteomes:UP000291562};
RA   Wei Z., Peng F.;
RT   "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT   Peninsula, Antarctica.";
RL   Submitted (JAN-2019) 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};
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DR   EMBL; CP035704; QBB69944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411HHR4; -.
DR   KEGG; xbc:ELE36_05970; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000291562; Chromosome.
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; 2.10.70.100; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; 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; PF13188; PAS_8; 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; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000291562}.
FT   DOMAIN          47..89
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          172..244
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          247..299
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          401..454
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          472..693
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          711..831
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          852..967
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         765
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         901
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   971 AA;  107510 MW;  C8770FA901499162 CRC64;
     MTDAITVVLV IAVPLILLVV ALLSMRGAFT RMPQQQQLDS FAAIRAGKDE LRQALDALPL
     PLAWHNQRRE IEFWNRRALA MFGYAPEEID TMDKWNALAY PDPDYRREMI KRWAAVEGEG
     ADGIRRDEFD ITCKDGRVIT VEISGTRDGD LTIVAFNDIT ERKGADEALR AMSTRLQLAV
     ASANTGIFDW DLVTNEVVWD DAMCRMYGIE QEDFNGFVTG WSEAVHPQDL PRVEAALQTA
     MHGGPEYYEE YRIRWPDGTE HHIMAYGQTT RDADGRPMRM VGASYDITER KLAEAELRRH
     RDHLEELVAE RTAQLQRVNL FNEQAMDLTR TGYWFVPLDD SGFYTNSDRA AAIYGVPAKP
     GDWRYNLMEE WYCHMESADP VIAAQVSEKF TKTCSGELPF YDAVYPFLRP VDGKIAWMHA
     MGIVVNDPKR PCREMYGVVQ DITEIIEAKR ELEEARAAAE AANQAKSAFL ATMSHEIRTP
     LNAILGMSHL ALKERTESER RSYLEKIQRA GQHLLAVIND VLDISKIEAG RLTIETAHFA
     LAELLDNAAN VTADRAAVKG LRFSVEVAAD VPAELVGDQL RLGQVLINYA TNAVKFTERG
     EITISVSVDS RTLHDAVLRF CVRDTGIGLT ADQIDNVFDA FQQGDSSITR RYGGTGLGLA
     ICRNLVRLMG GEMGVDSRLG VGSTFWFTAP VGIDGLQRRA VQLAPDLYGR RFLVAAGTGA
     ESANLSALLT GMRFTVVSAT DAEDTITILR ESISSGRSFD IVLLDIETFG SAGFAVAAQI
     KTLSSALKQR IVLVNSAERQ DLKKQAERSG YPTIDRPFDS STLFDRLVSM LGLADAAGIG
     NAESIKALHG ARVLVAEDNE FNQEVARAIL GDAGLVVDIA DDGEAAVRMV MASHYDAVLM
     DMQMPTMDGL TATRQIRSSV SAELPIIAMT ANAMQDNLQR CLDAGMDDFV AKPIDPDQLL
     VVLARWIKRR E
//
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