ID A0A1H3Y1E3_9BACT Unreviewed; 1357 AA.
AC A0A1H3Y1E3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05192529_10754 {ECO:0000313|EMBL:SEA05555.1};
OS Arachidicoccus rhizosphaerae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=551991 {ECO:0000313|EMBL:SEA05555.1, ECO:0000313|Proteomes:UP000199041};
RN [1] {ECO:0000313|EMBL:SEA05555.1, ECO:0000313|Proteomes:UP000199041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vu-144 {ECO:0000313|EMBL:SEA05555.1,
RC ECO:0000313|Proteomes:UP000199041};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNQY01000007; SEA05555.1; -; Genomic_DNA.
DR STRING; 551991.SAMN05192529_10754; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000199041; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:SEA05555.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199041};
KW Transferase {ECO:0000313|EMBL:SEA05555.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 773..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 826..1058
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1107..1222
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1254..1352
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1063..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1155
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1357 AA; 153986 MW; E1B0ABC42D4A355E CRC64;
MKSLFYLWIL FGLIAVARAQ DIQFRKLTSN QGLSHNTVYG ICQDDKGQMW FATREGLDRY
DSYQIKNYYI KDSLPGISPD KIGALLCDHD SIYIATEDGL YIYNQQSDQI SRSRALKQKL
SVLCLLKAGK VLFVGGTTGL FKLEAGKSEA ITQPNLTVRA MEQLGPDRFL ISIGNQIRVI
DGQGKTIKMF DGQSFTPLSI PNFDVYNMYK DQAGFVWLCT NYGLYYYDIN QQSFIRLHFS
ARDTREISTV RAIASDGKDL LYIGTENGLY IYHRSTGQAE NYGQSFDNNA KKLNDKAIYS
AFIARDGSVW LGTYFGGINY IPSNTYAFER IMPQDNGGGV SGKAVSQMME DSSHQIWIGT
EDGGITIYDP LKDQYSYINK TSRPFYLGIN NVHAIHSDGM GDIWVGTFLG GLHRFDLKNK
TTTIYTNKPG DSTSLSSDNV YAVYRDSRGT LWIGTQNGVN IFDYPKGRFK HFRSDVFSYK
FIYDIGEDQN GDIWFCTRFD GIYRYNPMGG TLNHYGATGP HPVLTSNQII SFYKDSKSNL
WFGTLGGGIL RFDFQKDTFK SYTTAEGLPN NNVYGILEDG AGYVWLTTNR GLSKYSPETD
RFINYNNKYG LPSNQFNFKS YLKTKDGTLY FGSINGLLFF HPEKIAARHP LVPLIFTDFQ
LFNKTVVPAE GAVLHRQIDY TRNIYLNYNQ NVFTINYAAI DYANPGSTHY AYYLKGFEDK
WNYVDGKNSV TYTNLSPGSY TFYVVALSAD GALQSVQRSI DIIVRPPFYR TKLAYLGYFL
LLLLLIWLYT RFIRFLHQKK MEVLIERIEK EKTKELTQNR LNFFTFISHE FKTPLTLILA
SIEKLISEKG DALKNNKELA GIKNSASVLF KLIQQLMEFR KVETGHNSVQ LSRADIVGFL
REATAYFDTM AISKGIDLQF SASCPELFAY FDKDKLEKIL FNILSNAIKN TQKGKITLRV
DCLSGRTETE DLEPASTQIT TKRDAAIAIS VIDTGQGMTR SELKNIFNPF YKAPDSELGS
GIGLSLVHSL VQYLNGVIAI ESEVQKGTTI SIKLPVVLKL EEKQPKKDMA PHKEGPSRAD
NNKLSLPEKR LTPENPAAII TEAKRYTLLI VEDNKELMVF LSNHFANFYH VISALNGQSA
LRKIAKLPPD IIISDVKMPK MDGIELCRHI KNNPKLSYLP VILLSEWESD EKRVTGLNTG
ADAYLGKPFN LKELELLVSN MIKSRVKLRE HVISISELAI DHLPTNNKNQ EFLTNLSNLL
EKRFQDSDFT IENMARDLNM SRTSLHLHLK KSMGKSASEL LNEYRLKRAA VMLENDMPIN
EAAYACGYND PNYFSRVFKK YYGQTPAKYR EQAKAEK
//
